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Ex.: O00571, ddx3x (keyword), ATP-dependent RNA helicase DDX3X, PXD000680 or 3JRV

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PDB 
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Phospho-sites

Showing 31 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
37 SER UP, PRIDE Combined
41 THR UP, PRIDE Combined
50 THR PRIDE yes
55 SER PRIDE yes
57 SER PRIDE yes
60 THR PRIDE yes
83 TYR PRIDE yes
95 THR PRIDE yes
97 SER UP Similarity
100 SER UP, PRIDE Similarity yes
105 TYR UP, PRIDE Combined yes
127 SER UP, PRIDE Combined yes
129 THR PRIDE yes
148 TYR UP, PRIDE Similarity yes
175 TYR UP, PRIDE Combined yes
182 SER PRIDE yes
195 THR UP Combined
202 SER PRIDE yes
205 SER PRIDE
222 SER PRIDE
249 SER PRIDE yes
269 SER PRIDE yes
287 SER PRIDE yes
333 SER PRIDE yes
346 SER PRIDE yes
370 TYR PRIDE yes
405 THR PRIDE
406 SER PRIDE
437 SER PRIDE yes
454 THR PRIDE yes
513 THR PRIDE yes

3D structure is not available

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Phosphorylated amino acids are colored red on the inner ring.

The first amino acid of the protein sequence is colored darker on each ring.

Phospho peptides

Showing 40 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
37 33 56 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
37 33 43 5 17
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 20 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD004252 7 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD000474 6 Simulated phosphopeptide spectral library for confident site localization Homo sapiens (Human) PARTIAL 2015-03-17 HeLa cell -
PXD003531 206 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD004940 11 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD001333 2 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD006482 6 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD002286 97 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD005366 203 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture -
PXD001550 59 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
PXD002394 18 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture -
PXD004452 75 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD001374 12 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell -
PXD000680 18 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
PXD000612 72 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001546 28 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD004415 27 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
41 33 56 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
50 44 56 7 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 2 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD001374 2 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell
PXD004452 3 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
55 44 56 12 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
57 44 62 14 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
57 57 62 1 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 1 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD003531 11 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD004940 1 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
60 57 62 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
83 74 89 10 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 3 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
95 93 115 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
100 93 115 8 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 3 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
105 93 115 13 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 6 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD001565 5 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003198 14 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
105 93 120 13 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 6 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003198 4 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
127 121 136 7 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
127 126 136 2 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 1 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD003531 2 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
PXD005366 3 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture -
127 126 135 2 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 57 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD003531 2 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
129 126 135 4 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 25 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD002286 4 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
148 142 162 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 15 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
148 142 151 7 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 18 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001565 4 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003198 16 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
175 174 206 2 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 19 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD002990 2 Complementary Phosphoproteomic Approaches Link IL-23R Downstream Signaling with Metabolic Adaptation in Lymphocytes Homo sapiens (Human) COMPLETE 2016-04-21 lymph node -
PXD005366 2 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture
PXD004452 31 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
175 174 186 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 1 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
182 174 206 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002436 1 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell
202 189 206 14 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD004452 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
205 189 224 17 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
222 189 224 34 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 3 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
222 208 224 15 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
249 247 256 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 24 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
249 247 255 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 15 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
269 267 278 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 2 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
287 280 305 8 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 5 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
333 320 336 14 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 3 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
346 343 367 4 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 4 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
PXD004452 3 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
370 343 376 28 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 1 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
370 368 376 3 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 4 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD001565 3 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
405 401 422 5 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000218 2 System-level analysis of cancer and stomal cell specific proteomes reveals extensive reprogramming of phosphorylation networks by tumor microenvironment Homo sapiens (Human),Mus musculus (Mouse) COMPLETE 2014-04-01 Epithelial cell, colon -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
406 400 422 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
406 401 422 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000218 2 System-level analysis of cancer and stomal cell specific proteomes reveals extensive reprogramming of phosphorylation networks by tumor microenvironment Homo sapiens (Human),Mus musculus (Mouse) COMPLETE 2014-04-01 Epithelial cell, colon
437 437 443 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 9 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
454 448 461 7 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
513 505 526 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon

Structures

Showing 32 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
6B6U A X-ray 1.350000023841858 4 [K]A:603 0.6429573 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 3.8823046684265137 0.0
41 41 THR C 0.79 70.32527160644531 0.0
45 45 THR C 1.0 0.3138123154640198 0.0
50 50 THR E 1.0 4.515092372894287 0.0
55 55 SER C 1.0 0.16589675843715668 0.0
57 57 SER C 0.91 55.77517318725586 0.0
60 60 THR H 0.34 33.31903076171875 0.0
83 83 TYR H 1.0 53.822322845458984 0.0
95 95 THR H 0.95 6.843642711639404 0.0
97 97 SER C 0.94 57.85030746459961 0.0
100 100 SER C 1.0 113.84960174560547 0.0
105 105 TYR C 0.92 20.60074806213379 0.0
127 127 SER C 1.0 87.74435424804688 0.0
129 129 THR C 1.0 124.12063598632812 0.0
148 148 TYR H 0.93 72.40524291992188 0.0
175 175 TYR E 0.95 55.041465759277344 0.0
182 182 SER E 1.0 4.0334696769714355 0.0
195 195 THR E 1.0 0.7355799674987793 0.0
202 202 SER E 0.63 59.861106872558594 0.0
205 205 SER C 1.0 21.37293815612793 0.0
222 222 SER C 1.0 33.44094467163086 0.0
249 249 SER H 0.49 55.58835220336914 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.9362852573394775 0.0
328 328 THR C 1.0 31.664505004882812 0.0
333 333 SER H 1.0 25.05025291442871 0.0
346 346 SER H 1.0 52.79836654663086 0.0
370 370 TYR C 1.0 61.97604751586914 0.0
405 405 THR C 0.46 69.69318389892578 0.0
406 406 SER C 0.37 112.40184020996094 0.0
409 409 THR H 0.3 9.659929275512695 0.0
412 412 THR H 0.46 30.495140075683594 0.0
437 437 TYR H 1.0 19.108840942382812 0.0
454 454 THR E 1.0 2.5246036052703857 0.0
513 513 THR C 0.93 3.9585976600646973 0.0
3GR4 A X-ray 1.600000023841858 4 B 0.5998849 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 4.259242057800293 1.172237515449524
41 41 THR C 0.79 67.58658599853516 0.0
45 45 THR C 1.0 0.1568174958229065 0.0
50 50 THR E 1.0 8.031181335449219 0.0
55 55 SER C 1.0 0.16348005831241608 0.0
57 57 SER C 0.91 53.02289581298828 0.0
60 60 THR H 0.34 31.451221466064453 0.0
83 83 TYR H 1.0 71.95143127441406 0.0
95 95 THR H 0.95 7.009576797485352 0.0
97 97 SER C 0.94 51.899166107177734 0.0
100 100 SER C 1.0 113.0941162109375 0.0
105 105 TYR C 0.92 17.979961395263672 0.0
127 127 SER E 1.0 47.00585174560547 0.0
129 129 THR C 1.0 128.10182189941406 0.0
148 148 TYR H 0.93 85.2929458618164 0.0
175 175 TYR E 0.95 55.770023345947266 0.0
182 182 SER E 1.0 6.948261737823486 0.0
195 195 THR E 1.0 1.7183895111083984 0.0
202 202 SER E 0.63 63.49544143676758 0.0
205 205 SER C 1.0 11.12417984008789 0.0
222 222 SER C 1.0 27.89877700805664 0.0
249 249 SER H 0.49 64.52996826171875 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.8386213779449463 0.0
328 328 THR C 1.0 34.19132614135742 2.5594797134399414
333 333 SER H 1.0 35.40686798095703 0.0
346 346 SER H 1.0 52.75872802734375 45.761470794677734
370 370 TYR C 1.0 61.94700622558594 0.0
405 405 THR C 0.46 63.36238098144531 0.0
406 406 SER C 0.37 108.69496154785156 0.0
409 409 THR H 0.3 15.924137115478516 0.0
412 412 THR H 0.46 17.765399932861328 0.0
437 437 SER H 1.0 14.912075996398926 0.0
454 454 THR E 1.0 2.8436391353607178 0.0
513 513 THR E 0.93 7.155914306640625 0.0
3GQY A X-ray 1.850000023841858 4 B 0.60642153 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 5.985180854797363 1.664171814918518
41 41 THR C 0.79 65.6897201538086 0.0
45 45 THR C 1.0 0.1568174958229065 0.0
50 50 THR E 1.0 6.690907955169678 0.0
55 55 SER C 1.0 0.16348005831241608 0.0
57 57 SER C 0.91 52.739044189453125 0.0
60 60 THR H 0.34 31.296459197998047 0.0
83 83 TYR H 1.0 73.53531646728516 0.0
95 95 THR H 0.95 6.513087272644043 0.0
97 97 SER C 0.94 51.992435455322266 0.0
100 100 SER C 1.0 113.85205841064453 0.0
105 105 TYR C 0.92 18.239322662353516 0.0
127 127 SER E 1.0 46.67670440673828 0.0
129 129 THR C 1.0 126.2805404663086 0.0
148 148 TYR H 0.93 95.9244384765625 0.0
175 175 TYR E 0.95 58.20063400268555 1.725157618522644
182 182 SER E 1.0 3.5195934772491455 0.0
195 195 THR E 1.0 4.6221394538879395 0.0
202 202 SER E 0.63 64.66426849365234 0.0
205 205 SER C 1.0 10.994062423706055 0.0
222 222 SER C 1.0 27.283164978027344 0.0
249 249 SER H 0.49 63.37460708618164 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 3.049635648727417 0.0
328 328 THR C 1.0 33.54035186767578 3.0492467880249023
333 333 SER H 1.0 31.354293823242188 0.0
346 346 SER H 1.0 52.75617599487305 47.223018646240234
370 370 TYR C 1.0 61.51539611816406 0.0
405 405 THR C 0.46 68.02446746826172 0.0
406 406 SER C 0.37 107.85559844970703 0.0
409 409 THR H 0.3 17.580219268798828 0.0
412 412 THR H 0.46 17.48641586303711 0.0
437 437 SER H 1.0 14.48381233215332 0.0
454 454 THR E 1.0 3.178637981414795 0.0
513 513 THR E 0.93 5.795377731323242 0.0
3ME3 A X-ray 1.9500000476837158 4 B 0.4731578 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 5.292839050292969 1.4522300958633423
41 41 THR C 0.79 64.66221618652344 0.0
45 45 THR C 1.0 0.1568174958229065 0.0
50 50 THR E 1.0 5.350706577301025 0.0
55 55 SER C 1.0 0.16348005831241608 0.0
57 57 SER C 0.91 51.423126220703125 0.0
60 60 THR H 0.34 31.802045822143555 0.0
83 83 TYR H 1.0 72.85700988769531 0.0
95 95 THR H 0.95 6.802894592285156 0.0
97 97 SER C 0.94 54.11480712890625 0.0
100 100 SER C 1.0 114.18656921386719 0.0
105 105 TYR C 0.92 18.588104248046875 0.0
127 127 SER E 1.0 40.311668395996094 0.0
129 129 THR C 1.0 124.31692504882812 0.0
148 148 TYR H 0.93 88.5160903930664 0.0
175 175 TYR E 0.95 58.792449951171875 2.663039445877075
182 182 SER E 1.0 8.448390007019043 0.0
195 195 THR E 1.0 1.564068078994751 0.0
202 202 SER E 0.63 64.4937515258789 0.0
205 205 SER C 1.0 11.263566970825195 0.0
222 222 SER C 1.0 28.429607391357422 0.0
249 249 SER H 0.49 63.94474411010742 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 3.1342384815216064 0.0
328 328 THR C 1.0 33.16312789916992 3.2179055213928223
333 333 SER H 1.0 33.421913146972656 1.8414422273635864
346 346 SER H 1.0 53.875244140625 48.04222869873047
370 370 TYR C 1.0 62.971832275390625 0.0
405 405 THR C 0.46 75.08950805664062 0.0
406 406 SER C 0.37 107.75700378417969 0.0
409 409 THR H 0.3 18.108125686645508 0.0
412 412 THR H 0.46 17.204395294189453 0.0
437 437 SER H 1.0 18.29764175415039 0.0
454 454 THR E 1.0 2.005614995956421 0.0
513 513 THR E 0.93 7.098898410797119 0.0
3BJF A X-ray 2.0299999713897705 4 [K]A:601 0.5587577 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 2.2758965492248535 0.0
41 41 THR C 0.79 71.87821197509766 0.0
45 45 THR C 1.0 0.15747712552547455 0.0
50 50 THR E 1.0 4.696722030639648 0.0
55 55 SER C 1.0 0.16863153874874115 0.0
57 57 SER C 0.91 49.568939208984375 0.0
60 60 THR H 0.34 46.587642669677734 0.0
83 83 TYR H 1.0 75.37393951416016 0.0
95 95 THR H 0.95 6.513652324676514 0.0
97 97 SER C 0.94 57.651084899902344 0.0
100 100 SER C 1.0 112.81498718261719 0.0
105 105 TYR C 0.92 18.899232864379883 0.0
127 127 SER C 1.0 66.87824249267578 0.0
129 129 THR C 1.0 121.09502410888672 0.0
148 148 TYR H 0.93 74.05680084228516 0.0
175 175 TYR E 0.95 52.69308090209961 0.0
182 182 SER E 1.0 4.112916469573975 0.0
195 195 THR E 1.0 0.0 0.0
202 202 SER E 0.63 54.10062026977539 0.0
205 205 SER C 1.0 23.475719451904297 0.0
222 222 SER C 1.0 29.4742374420166 0.0
249 249 SER H 0.49 51.967079162597656 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 3.4739153385162354 0.0
328 328 THR C 1.0 27.5771427154541 5.9018402099609375
333 333 SER H 1.0 19.286069869995117 0.0
346 346 SER H 1.0 54.774131774902344 0.0
370 370 TYR C 1.0 64.78875732421875 0.0
405 405 THR C 0.46 83.82221984863281 0.0
406 406 SER C 0.37 108.1802749633789 0.0
409 409 THR H 0.3 11.970338821411133 0.0
412 412 THR H 0.46 18.108556747436523 0.0
437 437 SER H 1.0 14.650206565856934 0.0
454 454 THR E 1.0 4.679455280303955 0.0
513 513 THR E 0.93 6.439050674438477 0.0
5X1V A X-ray 2.0999999046325684 4 B 0.46134555 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 5.630979537963867 1.1383662223815918
41 41 THR C 0.79 74.2423095703125 0.0
45 45 THR C 1.0 0.7829635739326477 0.0
50 50 THR E 1.0 5.691333770751953 0.0
55 55 SER C 1.0 0.16348005831241608 0.0
57 57 SER C 0.91 52.743553161621094 0.0
60 60 THR H 0.34 28.439552307128906 0.0
83 83 TYR H 1.0 69.5594253540039 0.0
95 95 THR H 0.95 5.344499588012695 0.0
97 97 SER C 0.94 55.74761962890625 0.0
100 100 SER C 1.0 111.69693756103516 0.0
105 105 TYR C 0.92 17.14742088317871 0.0
127 127 SER E 1.0 52.594932556152344 0.0
129 129 THR C 1.0 130.2925567626953 0.0
148 148 TYR H 0.93 80.52754974365234 0.0
175 175 TYR E 0.95 48.16291427612305 22.844295501708984
182 182 SER E 1.0 3.425413131713867 0.16729053854942322
195 195 THR E 1.0 1.2541145086288452 0.0
202 202 SER E 0.63 54.32098388671875 0.0
205 205 SER C 1.0 9.39416790008545 0.0
222 222 SER C 1.0 27.698965072631836 0.0
249 249 SER H 0.49 63.63423538208008 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.8260576725006104 0.0
328 328 THR C 1.0 31.635639190673828 3.253495693206787
333 333 SER H 1.0 30.048410415649414 0.0
346 346 SER H 1.0 52.44865417480469 46.69259262084961
370 370 TYR C 1.0 73.61314392089844 0.0
405 405 THR C 0.46 76.41368103027344 0.0
406 406 SER C 0.37 118.27637481689453 0.0
409 409 THR H 0.3 14.975727081298828 0.0
412 412 THR H 0.46 13.489075660705566 0.0
437 437 SER H 1.0 16.191205978393555 0.0
454 454 THR E 1.0 1.5017950534820557 0.0
513 513 THR E 0.93 6.768200397491455 0.0
3U2Z A X-ray 2.0999999046325684 4 [FBP]A:541 0.5727902 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 5.538995742797852 0.0
41 41 THR C 0.79 68.33287048339844 0.0
45 45 THR C 1.0 0.31429460644721985 0.0
50 50 THR E 1.0 5.015491008758545 0.0
55 55 SER C 1.0 0.16348005831241608 0.0
57 57 SER C 0.91 53.297611236572266 0.0
60 60 THR H 0.34 28.930566787719727 0.0
83 83 TYR H 1.0 77.32920837402344 0.0
95 95 THR H 0.95 6.834530353546143 0.0
97 97 SER C 0.94 54.44291305541992 0.0
100 100 SER C 1.0 111.12265014648438 0.0
105 105 TYR C 0.92 20.732391357421875 0.0
127 127 SER E 1.0 44.68339538574219 0.0
129 129 THR C 1.0 99.90168762207031 0.0
148 148 TYR H 0.93 102.92420959472656 0.0
175 175 TYR E 0.95 61.27608871459961 0.0
182 182 SER E 1.0 12.888945579528809 0.0
195 195 THR E 1.0 2.63493013381958 0.0
202 202 SER E 0.63 73.22735595703125 0.0
205 205 SER C 1.0 9.445446968078613 0.0
222 222 SER C 1.0 30.387645721435547 0.0
249 249 SER H 0.49 63.762733459472656 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.5219943523406982 0.0
328 328 THR C 1.0 34.676979064941406 0.0
333 333 SER H 1.0 28.35607147216797 0.0
346 346 SER H 1.0 52.73786163330078 0.0
370 370 TYR C 1.0 65.00435638427734 0.0
405 405 THR C 0.46 68.21292877197266 0.0
406 406 SER C 0.37 114.9027328491211 0.0
409 409 THR H 0.3 10.575942039489746 0.0
412 412 THR H 0.46 16.183984756469727 0.0
437 437 SER H 1.0 15.196575164794922 13.828160285949707
454 454 THR E 1.0 2.7529356479644775 0.0
513 513 THR E 0.93 7.862170219421387 0.6678152084350586
4B2D A X-ray 2.299999952316284 4 B 0.5784537 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 6.582272052764893 1.8442270755767822
41 41 THR C 0.79 53.49351501464844 0.0
45 45 THR C 1.0 0.0 0.0
50 50 THR E 1.0 5.855508804321289 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 54.04049301147461 0.0
60 60 THR H 0.34 28.56869125366211 0.0
83 83 TYR H 1.0 71.53627014160156 0.0
95 95 THR H 0.95 6.498850345611572 0.0
97 97 SER C 0.94 54.71011734008789 0.0
100 100 SER C 1.0 109.87725067138672 0.0
105 105 TYR C 0.92 19.62841033935547 0.0
127 127 SER E 1.0 47.542354583740234 0.0
129 129 THR C 1.0 128.55941772460938 0.0
148 148 TYR H 0.93 101.72055053710938 0.0
175 175 TYR E 0.95 58.584442138671875 7.723814010620117
182 182 SER E 1.0 1.4570198059082031 0.0
195 195 THR E 1.0 0.6254194974899292 0.0
202 202 SER E 0.63 65.9976577758789 0.0
205 205 SER C 1.0 9.185230255126953 0.0
222 222 SER C 1.0 27.231998443603516 0.0
249 249 SER H 0.49 64.36626434326172 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.980943202972412 0.0
328 328 THR C 1.0 34.755027770996094 2.3930108547210693
333 333 SER H 1.0 26.9333553314209 0.0
346 346 SER H 1.0 54.19781494140625 49.70165252685547
370 370 TYR C 1.0 62.31021499633789 0.0
405 405 THR C 0.46 76.7916259765625 0.0
406 406 SER C 0.37 113.03153991699219 0.0
409 409 THR H 0.3 11.467195510864258 0.0
412 412 THR H 0.46 15.704324722290039 0.0
437 437 SER H 1.0 13.678585052490234 0.0
454 454 THR E 1.0 2.008793830871582 0.0
513 513 THR E 0.93 9.029184341430664 0.0
4G1N A X-ray 2.299999952316284 4 B 0.6100742 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 5.0550537109375 1.9650485515594482
41 41 THR C 0.79 71.67045593261719 0.0
45 45 THR C 1.0 0.7829635739326477 0.0
50 50 THR E 1.0 6.015453338623047 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 54.815399169921875 0.0
60 60 THR H 0.34 34.76305389404297 0.0
83 83 TYR H 1.0 73.6181869506836 0.0
95 95 THR H 0.95 6.348607540130615 0.0
97 97 SER C 0.94 56.8762092590332 0.0
100 100 SER C 1.0 111.49479675292969 0.0
105 105 TYR C 0.92 16.144954681396484 0.0
127 127 SER C 1.0 79.68985748291016 0.0
129 129 THR C 1.0 144.71458435058594 0.0
148 148 TYR H 0.93 81.51974487304688 0.0
175 175 TYR E 0.95 51.944725036621094 0.0
182 182 SER E 1.0 4.985965251922607 0.0
195 195 THR E 1.0 0.0 0.0
202 202 SER E 0.63 61.63928985595703 0.0
205 205 SER C 1.0 43.19271469116211 0.0
222 222 SER C 1.0 27.254493713378906 0.0
249 249 SER H 0.49 51.19829177856445 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.7657976150512695 0.0
328 328 THR C 1.0 29.675884246826172 0.8289816975593567
333 333 SER H 1.0 31.68399429321289 0.0
346 346 SER H 1.0 53.841426849365234 47.815032958984375
370 370 TYR C 1.0 65.57325744628906 20.62550163269043
405 405 THR C 0.46 66.47899627685547 0.0
406 406 SER C 0.37 111.41606140136719 0.0
409 409 THR H 0.3 8.463111877441406 0.0
412 412 THR H 0.46 20.324974060058594 0.0
437 437 SER H 1.0 16.166515350341797 0.0
454 454 THR E 1.0 4.3564653396606445 0.0
513 513 THR E 0.93 4.792076110839844 0.0
4JPG A X-ray 2.3299999237060547 4 B 0.6781385 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 5.8101301193237305 1.2288892269134521
41 41 THR C 0.79 67.12887573242188 0.0
45 45 THR C 1.0 0.1568174958229065 0.0
50 50 THR E 1.0 6.192700386047363 0.0
55 55 SER C 1.0 0.16348005831241608 0.0
57 57 SER C 0.91 53.53000259399414 0.0
60 60 THR H 0.34 30.40566635131836 0.0
83 83 TYR H 1.0 77.3417739868164 0.0
95 95 THR H 0.95 6.881093502044678 0.0
97 97 SER C 0.94 57.654964447021484 0.0
100 100 SER C 1.0 110.6309585571289 0.0
105 105 TYR C 0.92 17.89472198486328 0.0
127 127 SER E 1.0 42.94376754760742 0.0
129 129 THR C 1.0 118.78775024414062 0.0
148 148 TYR H 0.93 88.77582550048828 0.0
175 175 TYR E 0.95 56.86015319824219 0.0
182 182 SER E 1.0 2.8777616024017334 0.0
195 195 THR E 1.0 1.1477562189102173 0.0
202 202 SER E 0.63 67.4832763671875 0.0
205 205 SER C 1.0 12.05077075958252 0.0
222 222 SER C 1.0 24.7416934967041 0.0
249 249 SER H 0.49 64.86445617675781 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.7665228843688965 0.0
328 328 THR C 1.0 33.468727111816406 2.4703621864318848
333 333 SER H 1.0 33.09865951538086 0.0
346 346 SER H 1.0 53.50289535522461 46.910335540771484
370 370 TYR C 1.0 67.67696380615234 0.0
405 405 THR C 0.46 66.07929229736328 0.0
406 406 SER C 0.37 115.3429183959961 0.0
409 409 THR H 0.3 13.227181434631348 0.0
412 412 THR H 0.46 16.462181091308594 0.0
437 437 SER H 1.0 13.9916410446167 0.0
454 454 THR E 1.0 2.1338677406311035 0.0
513 513 THR E 0.93 6.630006790161133 0.0
4YJ5 A X-ray 2.4100000858306885 4 B 0.66335446 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 5.584986686706543 1.7311241626739502
41 41 THR C 0.79 63.23065948486328 0.0
45 45 THR C 1.0 0.0 0.0
50 50 THR E 1.0 7.5284552574157715 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 57.5594596862793 0.0
60 60 THR H 0.34 33.646240234375 0.0
83 83 TYR H 1.0 75.90188598632812 0.0
95 95 THR H 0.95 7.139559745788574 0.0
97 97 SER C 0.94 50.714111328125 0.0
100 100 SER C 1.0 107.33712005615234 0.0
105 105 TYR C 0.92 22.279996871948242 0.0
127 127 SER C 1.0 116.58429718017578 0.0
129 129 THR C 1.0 108.24102783203125 0.0
148 148 TYR H 0.93 75.53255462646484 0.0
175 175 TYR E 0.95 54.25821304321289 1.097244143486023
182 182 SER E 1.0 4.566000461578369 0.0
195 195 THR E 1.0 0.3111917972564697 0.0
202 202 SER E 0.63 47.88141632080078 0.0
205 205 SER C 1.0 32.18842697143555 0.0
222 222 SER C 1.0 33.17636489868164 0.0
249 249 SER H 0.49 54.61298370361328 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.814547061920166 0.0
328 328 THR C 1.0 35.47111129760742 1.7255381345748901
333 333 SER H 1.0 29.90618133544922 0.0
346 346 SER H 1.0 53.8031005859375 47.293914794921875
370 370 TYR C 1.0 61.51078796386719 7.71832275390625
391 391 TYR H 1.0 13.880374908447266 0.0
405 405 THR C 0.46 101.22850036621094 0.0
406 406 SER C 0.37 51.31483840942383 0.0
409 409 THR H 0.3 10.371665954589844 0.0
412 412 THR H 0.46 21.109926223754883 0.0
437 437 SER H 1.0 12.745644569396973 0.0
454 454 THR E 1.0 3.520765781402588 0.0
513 513 THR E 0.93 4.852076053619385 0.0
6GG4 A X-ray 2.4600000381469727 4 [K]A:605 0.77040416 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 60.515625 0.0
41 41 THR C 0.79 26.577098846435547 0.0
45 45 THR C 1.0 0.24676232039928436 0.0
50 50 THR E 1.0 5.203847885131836 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 56.181949615478516 0.0
60 60 THR H 0.34 34.186302185058594 0.0
83 83 TYR H 1.0 75.25472259521484 0.0
95 95 THR H 0.95 6.959524631500244 0.0
97 97 SER C 0.94 53.78939437866211 0.0
100 100 SER C 1.0 110.15985870361328 0.0
105 105 TYR C 0.92 17.886823654174805 0.0
127 127 SER C 1.0 111.5333023071289 0.0
129 129 THR C 1.0 115.64231872558594 0.0
148 148 TYR H 0.93 88.14203643798828 0.0
175 175 TYR E 0.95 46.12281799316406 0.0
182 182 SER E 1.0 1.7517435550689697 0.0
195 195 THR E 1.0 0.9934940338134766 0.0
202 202 SER E 0.63 34.11797332763672 0.0
205 205 SER C 1.0 29.566043853759766 0.0
222 222 SER C 1.0 28.677120208740234 0.0
249 249 SER H 0.49 56.560096740722656 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 3.1321771144866943 0.0
328 328 THR C 1.0 33.2850341796875 0.0
333 333 SER H 1.0 37.18560791015625 0.0
346 346 SER H 1.0 41.463340759277344 0.0
370 370 TYR C 1.0 65.93460083007812 0.0
405 405 THR C 0.46 76.61238861083984 0.0
406 406 SER C 0.37 107.77220916748047 0.0
409 409 THR H 0.3 15.4553804397583 0.0
412 412 THR H 0.46 17.246097564697266 0.0
437 437 SER H 1.0 14.980094909667969 0.0
454 454 THR E 1.0 3.189314365386963 0.0
513 513 THR E 0.93 8.88601016998291 0.0
3BJT A X-ray 2.5 4 C 0.754163 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 5.284700393676758 4.712290287017822
41 41 THR C 0.79 102.5073013305664 0.0
45 45 THR C 1.0 0.46615880727767944 0.0
50 50 THR E 1.0 4.379061222076416 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 45.33259582519531 0.0
60 60 THR H 0.34 29.731176376342773 0.0
83 83 TYR H 1.0 73.9951171875 0.0
95 95 THR H 0.95 6.956583023071289 0.0
97 97 SER C 0.94 52.95528030395508 0.0
100 100 SER C 1.0 110.67552185058594 0.0
105 105 TYR C 0.92 23.805747985839844 0.0
127 127 SER C 1.0 87.3656234741211 0.0
129 129 THR C 1.0 92.94137573242188 0.0
148 148 TYR C 0.93 92.2125244140625 0.0
175 175 TYR E 0.95 54.227664947509766 1.4558446407318115
182 182 SER E 1.0 5.033348560333252 0.0
195 195 THR E 1.0 0.24432620406150818 0.0
202 202 SER E 0.63 56.6812858581543 0.0
205 205 SER C 1.0 24.656742095947266 0.0
222 222 SER C 1.0 37.16399002075195 0.0
249 249 SER H 0.49 62.318790435791016 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 3.9747774600982666 0.0
328 328 THR C 1.0 31.162723541259766 1.2368754148483276
333 333 SER H 1.0 22.373056411743164 0.0
346 346 SER H 1.0 57.057289123535156 48.80317687988281
370 370 TYR C 1.0 60.254512786865234 8.558100700378418
405 405 THR C 0.46 67.67945861816406 0.0
406 406 SER C 0.37 114.63023376464844 0.0
409 409 THR H 0.3 15.817133903503418 0.0
412 412 THR H 0.46 21.380176544189453 0.0
437 437 SER H 1.0 10.443693161010742 0.0
454 454 THR E 1.0 3.5218265056610107 0.0
513 513 THR E 0.93 7.271386623382568 0.0
4FXF A X-ray 2.549999952316284 4 [K]A:602 0.5796232 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 59.656028747558594 0.0
41 41 THR C 0.79 71.05595397949219 0.0
45 45 THR C 1.0 0.15747712552547455 0.0
50 50 THR E 1.0 4.183706283569336 0.0
55 55 SER C 1.0 0.16348005831241608 0.0
57 57 SER C 0.91 57.675323486328125 0.0
60 60 THR H 0.34 32.90071487426758 0.0
83 83 TYR H 1.0 72.3647689819336 0.0
95 95 THR H 0.95 7.183440685272217 0.0
97 97 SER C 0.94 55.36125946044922 0.0
100 100 SER C 1.0 109.76438903808594 0.0
105 105 TYR C 0.92 12.300085067749023 0.0
127 127 SER C 1.0 76.35968780517578 0.0
129 129 THR C 1.0 95.32125091552734 0.0
148 148 TYR H 0.93 91.0280990600586 0.0
175 175 TYR E 0.95 52.78596115112305 0.0
182 182 SER E 1.0 3.7286324501037598 0.0
195 195 THR E 1.0 0.5574362277984619 0.0
202 202 SER E 0.63 40.953033447265625 0.0
205 205 SER C 1.0 47.3303108215332 0.0
222 222 SER C 1.0 29.569011688232422 0.0
249 249 SER H 0.49 54.42150115966797 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.975301742553711 0.0
328 328 THR C 1.0 30.40594482421875 0.0
333 333 SER H 1.0 21.240070343017578 0.0
346 346 SER H 1.0 52.59722900390625 0.0
370 370 TYR C 1.0 66.5575942993164 0.0
405 405 THR C 0.46 74.18365478515625 0.0
406 406 SER C 0.37 114.44424438476562 0.0
409 409 THR H 0.3 6.358678817749023 0.0
412 412 THR H 0.46 14.07997989654541 0.0
437 437 SER H 1.0 12.488923072814941 0.0
454 454 THR E 1.0 2.005951404571533 0.0
513 513 THR E 0.93 7.181818962097168 0.0
5X0I A X-ray 2.640000104904175 4 [K]A:605 0.66975 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 6.048323631286621 0.0
41 41 THR C 0.79 64.35199737548828 0.0
45 45 THR C 1.0 0.0 0.0
50 50 THR E 1.0 6.865381240844727 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 53.673057556152344 0.0
60 60 THR H 0.34 31.169757843017578 0.0
83 83 TYR H 1.0 78.5559310913086 0.0
95 95 THR H 0.95 6.384679317474365 0.0
97 97 SER C 0.94 48.057979583740234 0.0
100 100 SER C 1.0 104.57194519042969 0.0
105 105 TYR C 0.92 26.392972946166992 0.0
127 127 SER C 1.0 70.07866668701172 0.0
129 129 THR C 1.0 129.25286865234375 0.0
148 148 TYR H 0.93 68.60604095458984 0.0
175 175 TYR E 0.95 53.071502685546875 0.0
182 182 SER E 1.0 3.284468173980713 0.0
195 195 THR E 1.0 0.9377747774124146 0.0
202 202 SER E 0.63 53.047359466552734 0.0
205 205 SER C 1.0 23.21174430847168 0.0
222 222 SER C 1.0 32.30936050415039 0.0
249 249 SER H 0.49 59.51638412475586 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.687385082244873 0.0
328 328 THR C 1.0 30.762733459472656 0.0
333 333 SER H 1.0 23.105756759643555 0.0
346 346 SER H 1.0 55.343406677246094 0.0
370 370 TYR C 1.0 59.10253143310547 0.0
405 405 THR C 0.46 73.65775299072266 0.0
406 406 SER C 0.37 115.91877746582031 0.0
409 409 THR H 0.3 9.126648902893066 0.0
412 412 THR H 0.46 18.149673461914062 0.0
437 437 SER H 1.0 12.778916358947754 0.0
454 454 THR E 1.0 4.735631465911865 0.0
513 513 THR E 0.93 9.573321342468262 0.0
1T5A A X-ray 2.799999952316284 4 [K]A:701 0.5635955 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 1.9124081134796143 0.0
41 41 THR C 0.79 80.27196502685547 0.0
45 45 THR C 1.0 0.4717717468738556 0.0
50 50 THR E 1.0 4.182388782501221 0.0
55 55 SER C 1.0 0.5008405447006226 0.0
57 57 SER C 0.91 51.39118576049805 0.0
60 60 THR H 0.34 42.16440200805664 0.0
83 83 TYR H 1.0 71.2765121459961 0.0
95 95 THR H 0.95 6.359621047973633 0.0
97 97 SER C 0.94 56.48552322387695 0.0
100 100 SER C 1.0 108.37935638427734 0.0
105 105 TYR C 0.92 13.52380084991455 0.0
127 127 SER C 1.0 64.12557220458984 0.0
129 129 THR C 1.0 129.3274688720703 0.0
148 148 TYR H 0.93 71.04743957519531 0.0
175 175 TYR E 0.95 54.42168045043945 0.0
182 182 SER E 1.0 4.030833721160889 0.0
195 195 THR E 1.0 0.0 0.0
202 202 SER E 0.63 60.578495025634766 0.0
205 205 SER C 1.0 21.391502380371094 0.0
222 222 SER C 1.0 23.799978256225586 0.0
249 249 SER H 0.49 55.640716552734375 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 4.769299030303955 0.0
328 328 THR C 1.0 30.300020217895508 0.0
333 333 SER H 1.0 26.474700927734375 0.0
346 346 SER H 1.0 56.54786682128906 0.0
370 370 TYR C 1.0 64.02290344238281 0.0
405 405 THR C 0.46 79.3028793334961 0.0
406 406 SER C 0.37 109.73114776611328 0.0
409 409 THR H 0.3 12.69823169708252 0.0
412 412 THR H 0.46 18.40767478942871 0.0
437 437 SER H 1.0 13.20553207397461 0.0
454 454 THR E 1.0 4.852232456207275 0.0
513 513 THR E 0.93 7.440695762634277 0.0
4WJ8 A X-ray 2.869999885559082 4 [K]A:603 0.5919518 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 6.788872718811035 0.0
41 41 THR C 0.79 92.10154724121094 0.0
45 45 THR C 1.0 0.15496699512004852 0.0
50 50 THR E 1.0 4.338857650756836 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 54.24263000488281 0.0
60 60 THR H 0.34 44.654727935791016 0.0
83 83 TYR H 1.0 72.22019958496094 0.0
95 95 THR H 0.95 6.916751861572266 0.0
97 97 SER C 0.94 53.959774017333984 0.0
100 100 SER C 1.0 111.42105865478516 0.0
105 105 TYR C 0.92 17.76056671142578 0.0
127 127 SER C 1.0 64.2469253540039 0.0
129 129 THR C 1.0 105.69393157958984 0.0
148 148 TYR H 0.93 73.54554748535156 0.0
175 175 TYR E 0.95 51.69037628173828 0.0
182 182 SER E 1.0 5.697903156280518 0.0
195 195 THR E 1.0 0.1549232304096222 0.0
202 202 SER E 0.63 43.464412689208984 0.0
205 205 SER C 1.0 45.68505859375 0.0
222 222 SER C 1.0 32.18107604980469 0.0
249 249 SER H 0.49 56.90096664428711 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.1308889389038086 0.0
328 328 THR C 1.0 30.12547492980957 0.0
333 333 SER H 1.0 18.606266021728516 0.0
346 346 SER H 1.0 54.22798156738281 0.0
370 370 TYR C 1.0 62.44807815551758 0.0
405 405 THR C 0.46 68.07190704345703 0.0
406 406 SER C 0.37 114.51309967041016 0.0
409 409 THR H 0.3 3.2197229862213135 0.0
412 412 THR H 0.46 19.104368209838867 0.0
437 437 SER H 1.0 10.589032173156738 0.0
454 454 THR E 1.0 5.356932640075684 0.0
513 513 THR E 0.93 6.17942476272583 0.0
6GG6 A X-ray 2.9600000381469727 4 [K]A:601 0.7383788 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 61.94512176513672 0.0
41 41 THR C 0.79 58.22355270385742 0.0
45 45 THR C 1.0 0.0 0.0
50 50 THR E 1.0 5.68873405456543 0.0
55 55 SER C 1.0 0.16729053854942322 0.0
57 57 SER C 0.91 58.942535400390625 0.0
60 60 THR H 0.34 33.048255920410156 0.0
83 83 TYR H 1.0 78.3818130493164 0.0
95 95 THR H 0.95 5.417573928833008 0.0
97 97 SER C 0.94 54.07018280029297 0.0
100 100 SER C 1.0 107.14623260498047 0.0
105 105 TYR C 0.92 11.464826583862305 0.0
127 127 SER C 1.0 113.23873901367188 0.0
129 129 THR C 1.0 107.0711669921875 0.0
148 148 TYR H 0.93 78.19055938720703 0.0
175 175 TYR E 0.95 53.796478271484375 0.0
182 182 SER E 1.0 2.520442485809326 0.0
195 195 THR E 1.0 0.9802062511444092 0.0
202 202 SER E 0.63 38.769737243652344 0.0
205 205 SER C 1.0 35.2353515625 0.0
222 222 SER C 1.0 22.32305908203125 0.0
249 249 SER H 0.49 52.89687728881836 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.220233201980591 0.0
328 328 THR C 1.0 23.47986602783203 0.0
333 333 SER H 1.0 21.660558700561523 0.0
346 346 SER H 1.0 56.206600189208984 0.0
370 370 TYR C 1.0 67.7008056640625 0.0
405 405 THR C 0.46 81.4586181640625 0.0
406 406 SER C 0.37 108.66433715820312 0.0
409 409 THR H 0.3 14.072558403015137 0.0
412 412 THR H 0.46 17.215112686157227 0.0
437 437 SER H 1.0 13.282144546508789 0.0
454 454 THR E 1.0 2.678959846496582 0.0
513 513 THR E 0.93 5.501550197601318 0.0
5X1W A X-ray 3.0 4 [FBP]A:601 0.5427889 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 6.788054943084717 0.0
41 41 THR C 0.79 72.95519256591797 0.0
45 45 THR C 1.0 1.8142154216766357 0.0
50 50 THR E 1.0 6.862284183502197 0.0
55 55 SER C 1.0 1.3200461864471436 0.0
57 57 SER C 0.91 49.64584732055664 0.0
60 60 THR H 0.34 30.238819122314453 0.0
83 83 TYR H 1.0 75.94010162353516 0.0
95 95 THR H 0.95 4.88478946685791 0.0
97 97 SER C 0.94 52.002567291259766 0.0
100 100 SER C 1.0 112.74346160888672 0.0
105 105 TYR C 0.92 9.804360389709473 0.0
127 127 SER E 1.0 38.125553131103516 0.0
129 129 THR C 1.0 129.74977111816406 0.0
148 148 TYR H 0.93 94.84701538085938 0.0
175 175 TYR E 0.95 50.9024658203125 0.0
182 182 SER E 1.0 3.6063661575317383 0.0
195 195 THR E 1.0 2.0863330364227295 0.0
202 202 SER E 0.63 53.64386749267578 0.0
205 205 SER C 1.0 11.279620170593262 0.0
222 222 SER C 1.0 22.823089599609375 0.0
249 249 SER H 0.49 65.39263916015625 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.1204066276550293 0.0
328 328 THR C 1.0 33.14649200439453 0.0
333 333 SER H 1.0 26.17998695373535 0.0
346 346 SER H 1.0 53.91387176513672 0.0
370 370 TYR C 1.0 74.80692291259766 0.0
405 405 THR C 0.46 79.1173324584961 0.0
406 406 SER C 0.37 116.30432891845703 0.0
409 409 THR H 0.3 16.375282287597656 0.0
412 412 THR H 0.46 17.020265579223633 0.0
437 437 SER H 1.0 16.355335235595703 10.541363716125488
454 454 THR E 1.0 1.1698660850524902 0.0
513 513 THR E 0.93 5.603866100311279 2.0108327865600586
6GG5 A X-ray 3.200000047683716 4 [K]A:605 0.7832723 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 127, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 58.437557220458984 0.0
41 41 THR C 0.79 21.695505142211914 0.0
45 45 THR C 1.0 0.4576440751552582 0.0
50 50 THR E 1.0 5.4625468254089355 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 58.18721389770508 0.0
60 60 THR H 0.34 32.7945671081543 0.0
83 83 TYR H 1.0 77.2925796508789 0.0
95 95 THR H 0.95 6.6980791091918945 0.0
97 97 SER C 0.94 49.58879089355469 0.0
100 100 SER C 1.0 110.49961853027344 0.0
105 105 TYR C 0.92 15.107168197631836 0.0
127 127 SER C 1.0 111.11978149414062 0.0
129 129 THR C 1.0 113.45681762695312 0.0
148 148 TYR H 0.93 78.91810607910156 0.0
175 175 TYR E 0.95 42.798152923583984 0.0
182 182 SER E 1.0 4.324246406555176 0.0
195 195 THR E 1.0 0.31731122732162476 0.0
202 202 SER E 0.63 34.69901657104492 0.0
205 205 SER C 1.0 35.87141799926758 0.0
222 222 SER C 1.0 25.42856788635254 0.0
249 249 SER H 0.49 53.523399353027344 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 3.8771750926971436 0.0
328 328 THR C 1.0 31.962688446044922 0.0
333 333 SER H 1.0 35.89754104614258 0.0
346 346 SER H 1.0 41.52577209472656 0.0
370 370 TYR C 1.0 71.99246978759766 0.0
405 405 THR C 0.46 68.7288589477539 0.0
406 406 SER C 0.37 106.71778869628906 0.0
409 409 THR H 0.3 17.07073402404785 0.0
412 412 THR H 0.46 20.49988555908203 0.0
437 437 SER H 1.0 13.026542663574219 0.0
454 454 THR E 1.0 3.025169849395752 0.0
513 513 THR E 0.93 4.268717288970947 0.0
4QG8 A X-ray 2.299999952316284 4 [K]A:1002 0.7136988 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 56.19213104248047 0.0
41 41 THR C 0.79 77.3346939086914 0.0
45 45 THR C 1.0 0.1562248170375824 0.0
50 50 THR E 1.0 6.507058143615723 0.0
55 55 SER C 1.0 0.3340039849281311 0.0
57 57 SER C 0.91 57.17729949951172 0.0
60 60 THR H 0.34 34.98326873779297 0.0
83 83 TYR H 1.0 77.25862884521484 0.0
95 95 THR H 0.95 6.882155895233154 0.0
97 97 SER C 0.94 53.89423751831055 0.0
100 100 SER C 1.0 108.36553955078125 0.0
105 105 TYR C 0.92 17.26424789428711 0.0
148 148 TYR C 0.93 83.61786651611328 0.0
175 175 TYR E 0.95 53.20939254760742 0.0
182 182 SER E 1.0 2.1747279167175293 0.0
195 195 THR E 1.0 0.3098464608192444 0.0
202 202 SER E 0.63 53.38570785522461 0.0
205 205 SER C 1.0 43.24509811401367 0.0
222 222 SER C 1.0 33.91737747192383 0.0
249 249 SER H 0.49 48.140933990478516 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 1.1738536357879639 0.0
328 328 THR C 1.0 28.52260398864746 0.0
333 333 SER H 1.0 31.840436935424805 0.0
346 346 SER H 1.0 51.997955322265625 0.0
370 370 TYR C 1.0 64.8335952758789 0.0
405 405 THR C 0.46 81.02942657470703 0.0
406 406 SER C 0.37 118.31340789794922 0.0
409 409 THR H 0.3 3.701326608657837 0.0
412 412 THR H 0.46 17.2562313079834 0.0
437 437 SER H 1.0 5.317898273468018 0.0
454 454 THR E 1.0 4.850354194641113 0.0
513 513 THR E 0.93 7.987921714782715 0.0
3SRD A X-ray 2.9000000953674316 4 [K]A:534 0.6239657 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 2.350170373916626 0.0
41 41 THR C 0.79 92.7623062133789 0.0
45 45 THR C 1.0 0.46615880727767944 0.0
50 50 THR E 1.0 6.020848751068115 0.0
55 55 SER C 1.0 0.33655673265457153 0.0
57 57 SER C 0.91 52.6572265625 0.0
60 60 THR H 0.34 41.72062683105469 0.0
83 83 TYR H 1.0 76.68657684326172 0.0
95 95 THR H 0.95 5.430749416351318 0.0
97 97 SER C 0.94 52.69321823120117 0.0
100 100 SER C 1.0 110.70997619628906 0.0
105 105 TYR C 0.92 19.167274475097656 0.0
148 148 TYR H 0.93 80.02457427978516 0.0
175 175 TYR E 0.95 57.41591262817383 0.0
182 182 SER E 1.0 9.410046577453613 0.0
195 195 THR E 1.0 0.0 0.0
202 202 SER E 0.63 49.9951171875 0.0
205 205 SER C 1.0 47.339088439941406 0.0
222 222 SER C 1.0 31.954265594482422 0.0
249 249 SER H 0.49 56.32741165161133 0.0
269 269 SER E 1.0 0.12296320497989655 0.0
287 287 SER C 1.0 2.788011074066162 0.0
328 328 THR C 1.0 30.185731887817383 0.0
333 333 SER H 1.0 17.74787712097168 0.0
346 346 SER H 1.0 56.459842681884766 0.0
370 370 TYR C 1.0 63.25068283081055 0.0
405 405 THR C 0.46 69.79058074951172 0.0
406 406 SER C 0.37 115.53417205810547 0.0
409 409 THR H 0.3 12.969706535339355 0.0
412 412 THR H 0.46 18.023046493530273 0.0
437 437 SER H 1.0 13.401878356933594 0.0
454 454 THR E 1.0 5.435591220855713 0.0
513 513 THR E 0.93 7.905277252197266 0.0
4QGC A X-ray 2.299999952316284 4 [K]A:1001 0.6251784 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 129, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 52.779808044433594 0.0
41 41 THR C 0.79 73.14154815673828 0.0
45 45 THR C 1.0 1.928167462348938 0.0
50 50 THR E 1.0 4.682405948638916 0.0
55 55 SER C 1.0 0.7954146265983582 0.0
57 57 SER C 0.91 51.54117965698242 0.0
60 60 THR H 0.34 28.980440139770508 0.0
83 83 TYR H 1.0 68.15150451660156 0.0
95 95 THR H 0.95 6.5511369705200195 0.0
97 97 SER C 0.94 56.238426208496094 0.0
100 100 SER C 1.0 110.09380340576172 0.0
105 105 TYR C 0.92 14.183399200439453 0.0
129 129 THR C 1.0 134.5384521484375 0.0
148 148 TYR H 0.93 82.89104461669922 0.0
175 175 TYR E 0.95 45.01708221435547 0.0
182 182 SER E 1.0 2.6227009296417236 0.0
195 195 THR E 1.0 0.7459705471992493 0.0
202 202 SER E 0.63 34.61860656738281 0.0
205 205 SER C 1.0 39.785701751708984 0.0
222 222 SER C 1.0 30.893796920776367 0.0
249 249 SER H 0.49 50.66312026977539 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.4924027919769287 0.0
328 328 THR C 1.0 32.615394592285156 0.0
333 333 SER H 1.0 36.05973815917969 0.0
346 346 SER H 1.0 40.78481674194336 0.0
370 370 TYR C 1.0 64.26655578613281 0.0
409 409 THR H 0.3 6.405372142791748 0.0
412 412 THR H 0.46 15.7365083694458 0.0
437 437 SER H 1.0 10.996598243713379 0.0
454 454 THR E 1.0 3.172964572906494 0.0
513 513 THR E 0.93 11.844820976257324 0.0
3H6O A X-ray 2.0 4 B 0.5469369 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 175, 182, 195, 205, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 6.917581558227539 1.6621711254119873
41 41 THR C 0.79 64.97148895263672 0.0
45 45 THR C 1.0 0.1568174958229065 0.0
50 50 THR E 1.0 4.3512678146362305 0.0
55 55 SER C 1.0 0.16348005831241608 0.0
57 57 SER C 0.91 55.18806838989258 0.0
60 60 THR H 0.34 33.37049102783203 0.0
83 83 TYR H 1.0 74.08456420898438 0.0
95 95 THR H 0.95 6.550121784210205 0.0
97 97 SER C 0.94 56.11223602294922 0.0
100 100 SER C 1.0 109.83797454833984 0.0
105 105 TYR C 0.92 16.889793395996094 0.0
175 175 TYR E 0.95 53.03498840332031 0.0
182 182 SER E 1.0 14.962218284606934 0.0
195 195 THR E 1.0 45.90831756591797 0.0
205 205 SER C 1.0 84.50415802001953 0.0
222 222 SER C 1.0 29.357454299926758 0.0
249 249 SER H 0.49 59.69340896606445 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.6468310356140137 0.0
328 328 THR C 1.0 31.156604766845703 2.4231531620025635
333 333 SER H 1.0 33.382667541503906 0.0
346 346 SER H 1.0 51.42045593261719 45.2104606628418
370 370 TYR C 1.0 61.56014633178711 0.0
405 405 THR C 0.46 58.460350036621094 0.0
406 406 SER C 0.37 105.41338348388672 0.0
409 409 THR H 0.3 17.281448364257812 0.0
412 412 THR H 0.46 17.13247299194336 0.0
437 437 SER H 1.0 14.69937515258789 0.0
454 454 THR E 1.0 3.5140843391418457 0.0
513 513 THR E 0.93 7.749116897583008 0.0
4QG9 A X-ray 2.380000114440918 4 D 0.81673205 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 49.5427131652832 3.3057968616485596
41 41 THR C 0.79 43.04248809814453 0.0
45 45 THR C 1.0 1.6390976905822754 0.0
50 50 THR E 1.0 6.195361614227295 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 52.6219367980957 0.0
60 60 THR H 0.34 23.612125396728516 0.0
83 83 TYR H 1.0 74.2470703125 0.0
95 95 THR H 0.95 6.768806457519531 0.0
97 97 SER H 0.94 55.97139358520508 0.0
100 100 SER C 1.0 109.58724975585938 0.0
105 105 TYR C 0.92 19.790178298950195 0.0
148 148 TYR H 0.93 77.08291625976562 0.0
175 175 TYR E 0.95 58.25230407714844 0.0
182 182 SER E 1.0 11.34325885772705 0.0
195 195 THR E 1.0 0.1549232304096222 0.0
202 202 SER C 0.63 47.69527053833008 0.0
205 205 SER C 1.0 35.854530334472656 0.0
222 222 SER C 1.0 32.96587371826172 0.0
249 249 SER H 0.49 68.09243774414062 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 3.5098540782928467 0.0
328 328 THR C 1.0 34.29554748535156 0.0
333 333 SER H 1.0 34.18911361694336 0.0
346 346 SER H 1.0 42.97087478637695 33.07485580444336
370 370 TYR C 1.0 64.87399291992188 0.0
409 409 THR H 0.3 27.208799362182617 0.0
412 412 THR H 0.46 16.405298233032227 0.0
437 437 SER H 1.0 13.470849990844727 0.0
454 454 THR E 1.0 3.8432602882385254 0.0
513 513 THR E 0.93 6.122622013092041 0.0
4FXJ A X-ray 2.9000000953674316 4 D 0.6513376 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 148, 175, 182, 195, 202, 205, 222, 249, 269, 287, 333, 346, 370, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 59.781856536865234 2.2797129154205322
41 41 THR C 0.79 36.737281799316406 0.0
45 45 THR C 1.0 0.3340039849281311 0.0
50 50 THR E 1.0 4.9962592124938965 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 58.94878387451172 0.0
60 60 THR H 0.34 37.539573669433594 0.0
83 83 TYR H 1.0 71.88958740234375 0.0
95 95 THR H 0.95 5.622107028961182 0.0
97 97 SER C 0.94 53.04351806640625 0.0
100 100 SER C 1.0 105.12973022460938 0.0
105 105 TYR C 0.92 14.00483226776123 0.0
148 148 TYR H 0.93 83.50341796875 0.0
175 175 TYR E 0.95 52.404014587402344 0.0
182 182 SER E 1.0 3.7189478874206543 0.0
195 195 THR E 1.0 0.48485004901885986 0.0
202 202 SER E 0.63 43.40877151489258 0.0
205 205 SER C 1.0 41.70859146118164 0.0
222 222 SER C 1.0 32.173362731933594 0.0
249 249 SER H 0.49 58.656436920166016 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 1.4863886833190918 0.0
328 328 THR C 1.0 34.64262008666992 0.0
333 333 SER H 1.0 34.748836517333984 0.0
346 346 SER H 1.0 44.7194709777832 39.3876838684082
370 370 TYR C 1.0 72.87390899658203 0.0
409 409 THR H 0.3 3.234173536300659 0.0
412 412 THR H 0.46 18.471372604370117 0.0
437 437 SER H 1.0 12.01047420501709 0.0
454 454 THR E 1.0 4.163221836090088 0.0
513 513 THR E 0.93 4.823258876800537 0.0
3G2G A X-ray 2.0 4 B 0.4026752 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 175, 182, 202, 205, 222, 249, 269, 287, 333, 346, 370, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 5.6046528816223145 1.507846713066101
41 41 THR C 0.79 66.3069839477539 0.0
45 45 THR C 1.0 0.314347505569458 0.0
50 50 THR E 1.0 7.356686115264893 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 53.7236442565918 0.0
60 60 THR H 0.34 33.65012741088867 0.0
83 83 TYR H 1.0 79.68470764160156 0.0
95 95 THR H 0.95 6.086361885070801 0.0
97 97 SER C 0.94 54.507171630859375 0.0
100 100 SER C 1.0 113.54598236083984 0.0
105 105 TYR C 0.92 21.646841049194336 0.0
175 175 TYR E 0.95 56.409183502197266 0.31084123253822327
182 182 SER E 1.0 9.067716598510742 0.0
202 202 SER C 0.63 100.29991149902344 0.0
205 205 SER C 1.0 106.9203109741211 0.0
222 222 SER C 1.0 32.28420639038086 0.0
249 249 SER H 0.49 53.25120544433594 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 3.562734365463257 0.0
328 328 THR C 1.0 32.23078918457031 2.2658140659332275
333 333 SER H 1.0 31.70677375793457 0.0
346 346 SER H 1.0 52.36083221435547 47.412288665771484
370 370 TYR C 1.0 59.66574478149414 5.158014297485352
409 409 THR H 0.3 49.133934020996094 0.0
412 412 THR H 0.46 22.374826431274414 0.0
437 437 TYR H 1.0 24.48355484008789 0.0
454 454 THR E 1.0 2.1698834896087646 0.0
513 513 THR C 0.93 13.47654914855957 0.0
4RPP A X-ray 2.5799999237060547 4 B 0.65847933 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 105, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 58.994503021240234 1.7183778285980225
41 41 THR C 0.79 64.00601196289062 0.0
45 45 THR C 1.0 1.1775068044662476 0.0
50 50 THR E 1.0 5.696007251739502 0.0
55 55 SER C 1.0 0.0 0.0
57 57 SER C 0.91 57.73765563964844 0.0
60 60 THR H 0.34 30.463077545166016 0.0
83 83 TYR H 1.0 73.18567657470703 0.0
95 95 THR H 0.95 6.672183036804199 0.0
97 97 SER H 0.94 49.69053268432617 0.0
100 100 SER C 1.0 108.25255584716797 0.0
105 105 TYR C 0.92 11.282955169677734 0.0
222 222 SER C 1.0 30.15673828125 0.0
249 249 SER H 0.49 56.4918212890625 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 2.8582687377929688 0.0
328 328 THR C 1.0 25.56403923034668 0.0
333 333 SER H 1.0 23.464824676513672 0.0
346 346 SER H 1.0 45.534332275390625 39.226844787597656
370 370 TYR C 1.0 69.21082305908203 0.0
405 405 THR C 0.46 57.1261100769043 0.0
406 406 SER C 0.37 110.71796417236328 0.0
409 409 THR H 0.3 24.760988235473633 0.0
412 412 THR H 0.46 17.366291046142578 0.0
437 437 SER H 1.0 14.382455825805664 0.0
454 454 THR E 1.0 1.1709647178649902 0.0
513 513 THR E 0.93 8.018911361694336 0.0
4QG6 A X-ray 3.2100000381469727 4 D 1.0 37, 41, 50, 55, 57, 60, 83, 95, 97, 100, 222, 249, 269, 287, 333, 346, 370, 405, 406, 437, 454, 513
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 37 SER C 1.0 66.13436889648438 3.1166069507598877
41 41 THR C 0.79 36.50900650024414 0.0
45 45 THR C 1.0 0.8949119448661804 0.0
50 50 THR E 1.0 2.8481228351593018 0.0
55 55 SER C 1.0 0.1443251669406891 0.0
57 57 SER C 0.91 47.280635833740234 0.0
60 60 THR H 0.34 44.11506652832031 0.0
83 83 TYR H 1.0 90.56827545166016 0.0
95 95 THR H 0.95 28.521800994873047 0.0
97 97 SER C 0.94 53.46244812011719 0.0
100 100 SER C 1.0 120.81902313232422 0.0
222 222 SER C 1.0 24.34554672241211 0.0
249 249 SER H 0.49 68.49414825439453 0.0
269 269 SER E 1.0 0.0 0.0
287 287 SER C 1.0 6.408174514770508 0.0
328 328 THR C 1.0 35.25707244873047 0.0
333 333 SER H 1.0 34.20191955566406 0.0
346 346 SER H 1.0 45.95130157470703 34.78034973144531
370 370 TYR C 1.0 73.70423889160156 0.0
405 405 THR C 0.46 73.1979751586914 0.0
406 406 SER C 0.37 103.00525665283203 0.0
409 409 THR H 0.3 15.862030982971191 0.0
412 412 THR H 0.46 16.4252872467041 0.0
437 437 SER H 1.0 10.531907081604004 0.0
454 454 THR E 1.0 3.6304636001586914 0.0
513 513 THR E 0.93 4.371038913726807 0.0
1ZJH A X-ray 2.200000047683716 4 A 1.0 406
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 36 SER C 1.0 60.827762603759766 1.704838752746582
41 40 THR C 0.79 41.339630126953125 0.0
45 44 THR C 1.0 0.2447987049818039 0.0
50 49 THR E 1.0 2.177833080291748 0.0
55 54 SER C 1.0 0.16526679694652557 0.0
57 56 SER C 0.91 44.03914260864258 0.0
60 59 THR H 0.34 32.76482009887695 0.0
83 82 TYR H 1.0 75.4079360961914 0.0
95 94 THR H 0.95 7.087212085723877 0.0
97 96 SER C 0.94 52.71015167236328 0.0
100 99 SER C 1.0 108.6629638671875 0.0
105 104 TYR C 0.92 23.942873001098633 0.0
127 126 SER C 1.0 69.64615631103516 0.0
129 128 THR C 1.0 134.67832946777344 0.0
148 147 TYR H 0.93 88.87248229980469 0.0
175 174 TYR E 0.95 38.221126556396484 7.652626991271973
182 181 SER E 1.0 8.37607192993164 0.0
195 194 THR E 1.0 6.732665061950684 0.0
202 201 SER C 0.63 59.60478210449219 0.0
205 204 SER C 1.0 8.811840057373047 0.0
222 221 SER C 1.0 30.143983840942383 0.0
249 248 SER H 0.49 62.18441390991211 0.0
269 268 SER E 1.0 0.0 0.0
287 286 SER C 1.0 2.61319637298584 0.0
328 327 THR C 1.0 26.19436264038086 4.046319007873535
333 332 SER C 1.0 25.79288101196289 0.0
346 345 SER H 1.0 58.38241195678711 50.38027572631836
370 369 TYR C 1.0 66.7656478881836 0.0
405 404 THR C 0.46 61.11199188232422 0.0
406 405 SER C 0.37 112.10186004638672 0.0
409 408 THR H 0.3 7.817883491516113 0.0
412 411 THR H 0.46 17.888206481933594 0.0
437 436 SER H 1.0 13.126708984375 0.0
454 453 THR E 1.0 2.1786322593688965 0.0
513 512 THR E 0.93 6.1887993812561035 0.0
3SRH A X-ray 2.5999999046325684 4 D 0.759433 406
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 36 SER C 1.0 7.723205089569092 1.9671626091003418
41 40 THR C 0.79 61.41129684448242 0.0
45 44 THR C 1.0 0.1568174958229065 0.0
50 49 THR E 1.0 4.296424865722656 0.0
55 54 SER C 1.0 0.32642418146133423 0.0
57 56 SER C 0.91 42.824378967285156 0.0
60 59 THR H 0.34 32.633975982666016 0.0
83 82 TYR H 1.0 75.87489318847656 0.0
95 94 THR H 0.95 6.295679092407227 0.0
97 96 SER C 0.94 51.30556106567383 0.0
100 99 SER C 1.0 110.28802490234375 0.0
105 104 TYR C 0.92 16.186378479003906 0.0
127 126 SER E 1.0 57.166080474853516 0.0
129 128 THR C 1.0 132.20315551757812 0.0
148 147 TYR H 0.93 83.01554107666016 0.0
175 174 TYR E 0.95 50.04408645629883 0.0
182 181 SER E 1.0 9.175786018371582 0.0
195 194 THR E 1.0 1.497659683227539 0.0
202 201 SER E 0.63 67.09456634521484 0.0
205 204 SER C 1.0 6.089867115020752 0.0
222 221 SER C 1.0 17.034353256225586 0.0
249 248 SER H 0.49 66.80021667480469 0.0
269 268 SER E 1.0 0.0 0.0
287 286 SER C 1.0 3.44836163520813 0.0
328 327 THR C 1.0 28.376585006713867 1.5908746719360352
333 332 SER H 1.0 29.377901077270508 0.0
346 345 SER H 1.0 59.292606353759766 52.59151840209961
370 369 TYR C 1.0 63.22053909301758 0.0
405 404 THR C 0.46 70.44895935058594 0.0
406 405 SER C 0.37 115.06568908691406 0.0
409 408 THR H 0.3 5.71298885345459 0.0
412 411 THR H 0.46 18.241910934448242 0.0
437 436 SER H 1.0 11.085325241088867 0.0
454 453 THR E 1.0 2.3478047847747803 0.0
513 512 THR E 0.93 6.770954608917236 0.0
3SRF A X-ray 2.8399999141693115 4 [K]A:532 0.63661206 406
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
37 36 SER C 1.0 2.8734233379364014 0.0
41 40 THR C 0.79 68.07025146484375 0.0
45 44 THR C 1.0 0.0 0.0
50 49 THR E 1.0 4.722370147705078 0.0
55 54 SER H 1.0 0.3360402584075928 0.0
57 56 SER C 0.91 45.54246139526367 0.0
60 59 THR H 0.34 33.88021469116211 0.0
83 82 TYR H 1.0 74.64507293701172 0.0
95 94 THR H 0.95 6.382512092590332 0.0
97 96 SER C 0.94 53.29755401611328 0.0
100 99 SER C 1.0 112.68111419677734 0.0
105 104 TYR C 0.92 24.993488311767578 0.0
129 128 THR C 1.0 197.67239379882812 0.0
148 147 TYR H 0.93 73.6258773803711 0.0
175 174 TYR E 0.95 56.8226203918457 0.0
182 181 SER E 1.0 5.656391143798828 0.0
195 194 THR E 1.0 1.429430603981018 0.0
202 201 SER E 0.63 43.94135284423828 0.0
205 204 SER C 1.0 42.9359245300293 0.0
222 221 SER C 1.0 24.191871643066406 0.0
249 248 SER H 0.49 63.93618392944336 0.0
269 268 SER E 1.0 0.0 0.0
287 286 SER C 1.0 1.9043022394180298 0.0
328 327 THR C 1.0 32.4677848815918 0.0
333 332 SER H 1.0 26.969152450561523 0.0
346 345 SER H 1.0 60.29648208618164 0.0
370 369 TYR C 1.0 65.19356536865234 0.0
405 404 SER C 0.46 44.233402252197266 0.0
406 405 THR C 0.37 122.94190979003906 0.0
437 436 SER H 1.0 6.952439785003662 0.0
454 453 THR E 1.0 3.126882314682007 0.0
513 512 THR E 0.93 6.107044696807861 0.0

Mutations

Showing 1 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
204 G V Polymorphism