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PDB 
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Phospho-sites

Showing 18 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
966 SER UP, PRIDE Combined yes
977 THR UP, PRIDE Combined yes
988 SER PRIDE
990 SER UP, PRIDE Combined
992 THR PRIDE
997 SER UP, PRIDE Combined
1000 SER UP, PRIDE Combined
1003 TYR UP, PRIDE Combined
1006 THR PRIDE
1230 TYR UP, PRIDE Experimental yes
1234 TYR UP, PRIDE Experimental
1235 TYR UP, PRIDE Experimental
1236 SER PRIDE
1257 THR PRIDE yes
1289 THR UP Combined
1349 TYR UP Experimental
1356 TYR UP, PRIDE Experimental yes
1365 TYR UP, PRIDE Experimental 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 25 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
966 963 970 4 7
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 3 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD002286 2 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD005366 17 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 2 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
966 963 974 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 5 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
977 971 982 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
977 975 982 3 11
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 1 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD004252 9 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
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 -
PXD004940 5 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD003531 17 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD001333 6 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 10 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 4 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD000680 1 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
988 988 1004 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
990 988 1004 3 11
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 5 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD004940 3 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD003531 10 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary 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
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 19 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 13 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD001550 1 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD003198 24 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
PXD000680 1 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
990 988 1022 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 3 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
992 988 1004 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
997 988 1004 10 4
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 -
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 -
PXD001550 19 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
PXD004452 3 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
1000 988 1004 13 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD005366 1 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 5 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
PXD001550 15 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD003198 4 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
1000 988 1022 13 2
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 -
PXD003198 4 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
1003 988 1004 16 4
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 -
PXD001550 1 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
PXD004452 3 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD003198 225 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
1003 988 1022 16 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 5 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
1006 988 1022 19 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
1230 1228 1240 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 2 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
1234 1228 1240 7 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 6 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD001565 36 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
PXD001550 3 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD003198 10 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
1234 1233 1240 2 4
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 -
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
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD003198 42 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
1235 1228 1240 8 4
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 -
PXD001565 8 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD001550 1 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
PXD003198 5 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
1235 1233 1244 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
1235 1233 1240 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 34 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
1236 1228 1240 9 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 4 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003198 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
1236 1233 1244 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003198 1 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
1257 1249 1259 9 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
1356 1337 1360 20 2
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 -
PXD003198 37 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
1365 1361 1390 5 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

Structures

Showing 74 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5UAB A X-ray 1.899999976158142 Monomer [CL]A:1403 0.077233285 1230, 1234, 1235, 1236, 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 69.7504653930664 0.0
1230 1230 TYR C 1.0 77.22367858886719 0.0
1234 1234 TYR H 0.97 18.63701629638672 0.0
1235 1235 TYR C 1.0 25.811010360717773 0.0
1236 1236 SER E 1.0 19.369487762451172 0.0
1257 1257 THR H 1.0 61.43292999267578 0.0
1289 1289 THR C 0.92 66.61969757080078 0.0
1349 1349 TYR E 0.89 117.79730987548828 0.0
1356 1356 TYR C 0.93 47.43132781982422 0.0
5UAF A X-ray 2.25 Monomer [CL]A:1402 0.087000795 1230, 1234, 1235, 1236, 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 66.60885620117188 0.0
1230 1230 TYR C 1.0 75.72920989990234 0.0
1234 1234 TYR H 0.97 18.2213077545166 0.0
1235 1235 TYR C 1.0 22.345823287963867 0.0
1236 1236 SER E 1.0 22.12552261352539 0.0
1257 1257 THR H 1.0 60.491249084472656 0.0
1289 1289 THR C 0.92 67.51467895507812 0.0
1349 1349 TYR E 0.89 116.94066619873047 0.0
1356 1356 TYR C 0.93 51.77058410644531 0.0
5UAD A X-ray 2.25 Monomer [CL]A:1402 0.087000795 1230, 1234, 1235, 1236, 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 66.60885620117188 0.0
1230 1230 TYR C 1.0 75.72920989990234 0.0
1234 1234 TYR H 0.97 18.2213077545166 0.0
1235 1235 TYR C 1.0 22.345823287963867 0.0
1236 1236 SER E 1.0 22.12552261352539 0.0
1257 1257 THR H 1.0 60.491249084472656 0.0
1289 1289 THR C 0.92 67.51467895507812 0.0
1349 1349 TYR E 0.89 116.94066619873047 0.0
1356 1356 TYR C 0.93 51.77058410644531 0.0
3F66 A X-ray 1.399999976158142 Monomer [GBL]A:4 0.0713438 1230, 1234, 1235, 1236, 1257, 1289, 1349
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 70.83285522460938 0.0
1230 1230 TYR C 1.0 84.55818176269531 0.0
1234 1234 TYR H 0.97 68.22801208496094 0.0
1235 1235 TYR C 1.0 28.12169647216797 0.0
1236 1236 SER E 1.0 33.161190032958984 0.0
1257 1257 THR H 1.0 80.99898529052734 0.0
1289 1289 THR C 0.92 48.986846923828125 0.0
1349 1349 TYR C 0.89 216.58580017089844 0.0
4R1V A X-ray 1.2000000476837158 Monomer [GBL]A:1402 0.044633027 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 79.47673034667969 0.0
1230 1230 TYR C 1.0 70.16341400146484 0.0
1234 1234 TYR H 0.97 31.09920883178711 0.0
1235 1235 TYR C 1.0 27.273706436157227 0.0
1236 1236 SER E 1.0 22.171415328979492 0.0
1257 1257 THR H 1.0 71.4581298828125 0.0
1289 1289 THR H 0.92 42.85059356689453 0.0
3ZCL A X-ray 1.399999976158142 Monomer A 0.0 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 63.63286590576172 0.0
1230 1230 TYR C 1.0 70.91680908203125 0.0
1234 1234 TYR H 0.97 35.290260314941406 0.0
1235 1235 TYR C 1.0 10.742950439453125 0.0
1236 1236 SER E 1.0 15.114206314086914 0.0
1257 1257 THR H 1.0 71.57366943359375 0.0
1289 1289 THR H 0.92 37.01559829711914 0.0
3DKC A X-ray 1.5199999809265137 Monomer [CL]A:3 0.04379555 1230, 1236, 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 72.65374755859375 0.0
1230 1230 TYR H 1.0 3.676295518875122 0.0
1236 1236 SER C 1.0 31.890609741210938 0.0
1257 1257 THR H 1.0 88.52588653564453 0.0
1289 1289 THR C 0.92 36.25444793701172 0.0
1349 1349 TYR E 0.89 105.99933624267578 0.0
1356 1356 TYR E 0.93 137.79212951660156 0.0
4MXC A X-ray 1.6299999952316284 Monomer [DWF]A:1401 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 68.61282348632812 16.665987014770508
1230 1230 TYR C 1.0 112.89482879638672 20.97916603088379
1234 1234 TYR H 0.97 41.37255859375 0.0
1235 1235 TYR C 1.0 13.795975685119629 0.0
1236 1236 SER E 1.0 47.64030838012695 0.0
1257 1257 THR H 1.0 83.20118713378906 0.0
1289 1289 THR C 0.92 140.07240295410156 0.0
5HTI A X-ray 1.659999966621399 Monomer [66L]A:1401 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 71.22116088867188 22.66208267211914
1230 1230 TYR C 1.0 116.30880737304688 0.4674166142940521
1234 1234 TYR C 0.97 26.392362594604492 0.0
1235 1235 TYR C 1.0 15.75067138671875 0.0
1236 1236 SER E 1.0 9.79663372039795 0.0
1257 1257 THR H 1.0 80.14270782470703 0.0
1289 1289 THR H 0.92 33.01793670654297 0.0
5EOB A X-ray 1.75 Monomer [5QQ]A:1401 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 80.03726196289062 5.9266743659973145
1230 1230 TYR C 1.0 75.70661926269531 58.655487060546875
1234 1234 TYR H 0.97 34.65529251098633 0.0
1235 1235 TYR C 1.0 30.859010696411133 0.0
1236 1236 SER E 1.0 43.476322174072266 0.0
1257 1257 THR H 1.0 85.80268096923828 0.0
1289 1289 THR H 0.92 52.8153076171875 0.0
4XMO A X-ray 1.75 Monomer [46G]A:1401 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 62.584922790527344 9.631566047668457
1230 1230 TYR C 1.0 75.84241485595703 59.4434700012207
1234 1234 TYR H 0.97 29.21709442138672 0.0
1235 1235 TYR C 1.0 22.01057243347168 0.0
1236 1236 SER E 1.0 17.214628219604492 0.0
1257 1257 THR H 1.0 91.8938217163086 0.0
1289 1289 THR H 0.92 68.34563446044922 0.0
3ZXZ A X-ray 1.7999999523162842 Monomer [KRW]A:2345 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 72.88705444335938 5.909193515777588
1230 1230 TYR C 1.0 70.25048828125 55.817466735839844
1234 1234 TYR H 0.97 35.361900329589844 0.0
1235 1235 TYR C 1.0 10.691126823425293 0.0
1236 1236 SER E 1.0 14.482268333435059 0.0
1257 1257 THR H 1.0 72.14311218261719 0.0
1289 1289 THR C 0.92 37.00534439086914 0.0
5EYC A X-ray 1.7999999523162842 Monomer [5SZ]A:1401 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 60.92974090576172 5.138920307159424
1230 1230 TYR C 1.0 73.8278579711914 59.43797302246094
1234 1234 TYR H 0.97 28.02463722229004 0.0
1235 1235 TYR C 1.0 21.589628219604492 0.0
1236 1236 SER E 1.0 19.53704261779785 0.0
1257 1257 THR H 1.0 87.76881408691406 0.0
1289 1289 THR H 0.92 71.12299346923828 0.0
4AP7 A X-ray 1.7999999523162842 Monomer [F47]A:2345 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 58.04433059692383 1.3269926309585571
1230 1230 TYR C 1.0 62.835330963134766 47.89351272583008
1234 1234 TYR H 0.97 35.61740493774414 0.0
1235 1235 TYR C 1.0 11.119501113891602 0.0
1236 1236 SER E 1.0 13.498688697814941 0.0
1257 1257 THR H 1.0 73.74688720703125 0.0
1289 1289 THR C 0.92 37.957725524902344 0.0
5EYD A X-ray 1.850000023841858 Monomer A 0.0 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 62.82242965698242 0.0
1230 1230 TYR C 1.0 74.04064178466797 0.0
1234 1234 TYR H 0.97 29.060644149780273 0.0
1235 1235 TYR C 1.0 22.888431549072266 0.0
1236 1236 SER E 1.0 17.491666793823242 0.0
1257 1257 THR H 1.0 92.06025695800781 0.0
1289 1289 THR H 0.92 71.27159118652344 0.0
4XYF A X-ray 1.850000023841858 Monomer A 0.0 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 67.82975769042969 0.0
1230 1230 TYR C 1.0 75.33081817626953 0.0
1234 1234 TYR H 0.97 28.91265106201172 0.0
1235 1235 TYR C 1.0 21.12812042236328 0.0
1236 1236 SER E 1.0 19.242015838623047 0.0
1257 1257 THR H 1.0 87.81641387939453 18.434236526489258
1289 1289 THR H 0.92 67.94141387939453 0.0
3ZZE A X-ray 1.8700000047683716 Monomer [6XP]A:2345 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 56.7187614440918 1.668901801109314
1230 1230 TYR C 1.0 71.07086944580078 55.829769134521484
1234 1234 TYR H 0.97 35.99835968017578 0.0
1235 1235 TYR C 1.0 13.489961624145508 0.0
1236 1236 SER E 1.0 14.805047988891602 0.0
1257 1257 THR H 1.0 71.08856964111328 0.0
1289 1289 THR C 0.92 36.4823112487793 0.0
3CCN A X-ray 1.899999976158142 Monomer A 0.0 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 54.58988952636719 0.0
1230 1230 TYR C 1.0 68.64385223388672 0.0
1234 1234 TYR H 0.97 28.329444885253906 0.0
1235 1235 TYR C 1.0 15.574996948242188 0.0
1236 1236 SER E 1.0 18.01881980895996 0.0
1257 1257 THR H 1.0 95.12373352050781 0.0
1289 1289 THR H 0.92 74.85393524169922 0.0
4AOI A X-ray 1.899999976158142 Monomer [4K0]A:2345 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 69.88288116455078 3.7109031677246094
1230 1230 TYR C 1.0 61.882198333740234 48.945411682128906
1234 1234 TYR H 0.97 36.10714340209961 0.0
1235 1235 TYR C 1.0 10.780021667480469 0.0
1236 1236 SER E 1.0 15.393267631530762 0.0
1257 1257 THR H 1.0 71.81817626953125 0.0
1289 1289 THR C 0.92 37.29595184326172 0.0
3RHK A X-ray 1.940000057220459 Monomer [M97]A:1 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 74.58158111572266 1.9824178218841553
1230 1230 TYR C 1.0 46.80256652832031 0.0
1234 1234 TYR C 0.97 60.840476989746094 0.0
1235 1235 TYR C 1.0 12.797783851623535 0.0
1236 1236 SER E 1.0 36.79571533203125 0.0
1257 1257 THR H 1.0 73.88462829589844 0.0
1289 1289 THR H 0.92 67.200927734375 0.0
5HLW A X-ray 1.9700000286102295 Monomer [CL]A:1401 0.056228425 1234, 1235, 1236, 1257, 1289, 1349
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 70.75630187988281 0.0
1234 1234 TYR C 0.97 29.64214324951172 0.0
1235 1235 TYR C 1.0 16.4642276763916 0.0
1236 1236 SER C 1.0 27.187667846679688 0.0
1257 1257 THR H 1.0 75.82640838623047 0.0
1289 1289 THR H 0.92 25.135202407836914 0.0
1349 1349 TYR E 0.89 115.29804229736328 0.0
3CD8 A X-ray 2.0 Monomer A 0.0 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 55.4713020324707 0.0
1230 1230 TYR C 1.0 73.18975067138672 0.0
1234 1234 TYR H 0.97 31.359577178955078 0.0
1235 1235 TYR C 1.0 17.06748390197754 0.0
1236 1236 SER E 1.0 16.360397338867188 0.0
1257 1257 THR H 1.0 93.6860580444336 0.0
1289 1289 THR H 0.92 71.97936248779297 0.0
4DEG A X-ray 2.0 Monomer A 0.0 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 54.1920166015625 0.0
1230 1230 TYR C 1.0 69.37274932861328 0.0
1234 1234 TYR H 0.97 29.506900787353516 0.0
1235 1235 TYR C 1.0 22.956771850585938 0.0
1236 1236 SER E 1.0 18.319503784179688 0.0
1257 1257 THR H 1.0 90.49454498291016 0.0
1289 1289 THR H 0.92 71.26232147216797 0.0
4R1Y A X-ray 2.0 Monomer [3EH]A:1401 0.11037807 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 82.04742431640625 13.55042552947998
1230 1230 TYR C 1.0 71.66021728515625 51.68457794189453
1234 1234 TYR H 0.97 29.542449951171875 0.0
1235 1235 TYR C 1.0 22.410367965698242 0.0
1236 1236 SER E 1.0 21.765714645385742 0.0
1257 1257 THR H 1.0 64.38214874267578 0.0
1289 1289 THR H 0.92 54.98274230957031 0.0
2WGJ A X-ray 2.0 Monomer [VGH]A:2346 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 56.323402404785156 20.600242614746094
1230 1230 TYR C 1.0 74.04969787597656 36.205177307128906
1234 1234 TYR H 0.97 38.423274993896484 0.0
1235 1235 TYR C 1.0 12.525153160095215 0.0
1236 1236 SER E 1.0 12.119394302368164 0.0
1257 1257 THR H 1.0 69.34640502929688 0.0
1289 1289 THR C 0.92 38.272926330566406 0.0
2WD1 A X-ray 2.0 Monomer [ZZY]A:2347 0.04027992 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 83.61443328857422 12.367961883544922
1230 1230 TYR C 1.0 75.46448516845703 39.69906997680664
1234 1234 TYR H 0.97 35.57455062866211 0.0
1235 1235 TYR C 1.0 28.475900650024414 0.0
1236 1236 SER E 1.0 19.584125518798828 0.0
1257 1257 THR H 1.0 83.3668212890625 0.0
1289 1289 THR H 0.92 56.9346923828125 0.0
3I5N A X-ray 2.0 Monomer A 0.0 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 59.371829986572266 0.0
1230 1230 TYR C 1.0 74.25100708007812 0.0
1234 1234 TYR H 0.97 30.289823532104492 0.0
1235 1235 TYR C 1.0 17.43294334411621 0.0
1236 1236 SER E 1.0 17.84213638305664 0.0
1257 1257 THR H 1.0 92.70765686035156 0.0
1289 1289 THR H 0.92 71.38187408447266 0.0
4DEH A X-ray 2.0 Monomer A 0.0 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 68.8424301147461 0.0
1230 1230 TYR C 1.0 78.13853454589844 0.0
1234 1234 TYR H 0.97 31.65748405456543 0.0
1235 1235 TYR C 1.0 24.336694717407227 0.0
1236 1236 SER E 1.0 16.53097915649414 0.0
1257 1257 THR H 1.0 92.72864532470703 0.0
1289 1289 THR H 0.92 74.52025604248047 0.0
4DEI A X-ray 2.049999952316284 Monomer [0JL]A:1401 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 55.832252502441406 19.71821403503418
1230 1230 TYR C 1.0 72.30779266357422 57.982608795166016
1234 1234 TYR H 0.97 27.77829933166504 0.0
1235 1235 TYR C 1.0 15.64676570892334 0.0
1236 1236 SER E 1.0 18.561731338500977 0.0
1257 1257 THR H 1.0 86.56977081298828 0.0
1289 1289 THR H 0.92 73.84786224365234 0.0
3VW8 A X-ray 2.0999999046325684 Monomer [CL]A:1402 0.075995296 1230, 1234, 1235, 1236, 1257, 1349
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 62.75105667114258 0.0
1230 1230 TYR H 1.0 162.501220703125 0.0
1234 1234 TYR H 0.97 22.816246032714844 0.0
1235 1235 TYR C 1.0 7.241434574127197 0.0
1236 1236 SER C 1.0 84.34909057617188 0.0
1257 1257 THR H 1.0 81.60957336425781 0.0
1349 1349 TYR E 0.89 129.42103576660156 0.0
2G15 A X-ray 2.1500000953674316 3 A 1.0 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 63.49338150024414 0.0
1230 1230 TYR C 1.0 151.02928161621094 0.0
1234 1234 TYR C 0.97 17.839279174804688 0.0
1235 1235 TYR C 1.0 76.61621856689453 0.0
1236 1236 SER C 1.0 8.307088851928711 0.0
1257 1257 THR H 1.0 76.39102935791016 0.0
1289 1289 THR H 0.92 64.6822280883789 0.0
3ZBX A X-ray 2.200000047683716 Monomer A 0.0 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 67.82971954345703 0.0
1230 1230 TYR C 1.0 66.11671447753906 0.0
1234 1234 TYR H 0.97 38.0710563659668 0.0
1235 1235 TYR C 1.0 10.73569107055664 0.0
1236 1236 SER E 1.0 16.116790771484375 0.0
1257 1257 THR H 1.0 72.77361297607422 0.0
1289 1289 THR C 0.92 38.514366149902344 0.0
2RFS A X-ray 2.200000047683716 Monomer [AM8]A:1 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 73.23735046386719 15.248058319091797
1230 1230 TYR C 1.0 86.03307342529297 40.92145919799805
1234 1234 TYR H 0.97 22.10098648071289 0.0
1235 1235 TYR C 1.0 19.602642059326172 0.0
1236 1236 SER E 1.0 21.819034576416016 0.0
1257 1257 THR H 1.0 94.1430435180664 0.0
1289 1289 THR H 0.92 72.02139282226562 0.0
2WKM A X-ray 2.200000047683716 Monomer [PFY]A:2345 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 63.152896881103516 14.513233184814453
1230 1230 TYR C 1.0 86.17874908447266 46.083473205566406
1234 1234 TYR C 0.97 52.95137405395508 0.0
1235 1235 TYR C 1.0 23.922679901123047 0.0
1236 1236 SER E 1.0 13.930767059326172 0.0
1257 1257 THR H 1.0 72.62651824951172 0.0
1289 1289 THR C 0.92 36.7318229675293 0.0
3ZC5 A X-ray 2.200000047683716 Monomer [W9Z]A:2345 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 79.27452850341797 6.04994535446167
1230 1230 TYR C 1.0 70.60128784179688 58.22682189941406
1234 1234 TYR H 0.97 36.061195373535156 0.0
1235 1235 TYR C 1.0 10.850449562072754 0.0
1236 1236 SER E 1.0 14.478316307067871 0.0
1257 1257 THR H 1.0 74.84386444091797 0.0
1289 1289 THR C 0.92 36.14385986328125 0.0
4GG7 A X-ray 2.2699999809265137 Monomer [0J8]A:1401 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 64.64729309082031 21.232311248779297
1230 1230 TYR C 1.0 84.38562774658203 46.89387512207031
1234 1234 TYR H 0.97 35.67209243774414 0.0
1235 1235 TYR C 1.0 26.383041381835938 0.0
1236 1236 SER E 1.0 50.7094612121582 0.0
1257 1257 THR H 1.0 88.17596435546875 0.0
1289 1289 THR C 0.92 70.7654800415039 0.0
4KNB A X-ray 2.4000000953674316 Monomer [1RU]A:1401 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 72.17605590820312 31.25676918029785
1230 1230 TYR C 1.0 76.4808578491211 41.853267669677734
1234 1234 TYR H 0.97 35.14308547973633 0.0
1235 1235 TYR C 1.0 21.312612533569336 0.0
1236 1236 SER E 1.0 25.250322341918945 0.0
1257 1257 THR H 1.0 80.49652099609375 0.0
1289 1289 THR C 0.92 39.59072494506836 0.0
4GG5 A X-ray 2.4200000762939453 Monomer [0J3]A:1401 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 69.4682846069336 18.559650421142578
1230 1230 TYR C 1.0 83.63861083984375 46.39525604248047
1234 1234 TYR H 0.97 35.38261795043945 0.0
1235 1235 TYR E 1.0 27.842750549316406 0.0
1236 1236 SER E 1.0 53.56263732910156 0.0
1257 1257 THR H 1.0 77.99732971191406 0.0
1289 1289 THR C 0.92 69.6795883178711 0.0
5DG5 A X-ray 2.5999999046325684 Monomer [5B4]A:1401 0.1 1230, 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 72.74705505371094 24.664997100830078
1230 1230 TYR C 1.0 191.38204956054688 0.0
1234 1234 TYR E 0.97 20.142898559570312 11.298501968383789
1235 1235 TYR E 1.0 86.28274536132812 0.0
1236 1236 SER E 1.0 32.680702209472656 0.0
1257 1257 THR H 1.0 88.1869888305664 0.0
1289 1289 THR C 0.92 65.6052017211914 0.0
5HNI X X-ray 1.7100000381469727 Monomer [63B]X:1401 0.1 1230, 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 77.45890808105469 27.980430603027344
1230 1230 TYR C 1.0 158.36981201171875 49.947628021240234
1257 1257 THR H 1.0 72.88835144042969 0.0
1289 1289 THR H 0.92 117.87935638427734 0.0
1349 1349 TYR E 0.89 115.63789367675781 0.0
1356 1356 TYR C 0.93 53.622520446777344 0.0
1R0P A X-ray 1.7999999523162842 Monomer [KSA]A:0 0.1 1230, 1236, 1257, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 64.46382141113281 14.146135330200195
1230 1230 TYR C 1.0 85.53948974609375 53.27275848388672
1236 1236 SER C 1.0 47.350345611572266 0.0
1257 1257 THR H 1.0 76.94085693359375 0.0
1349 1349 TYR E 0.89 117.80750274658203 0.0
1356 1356 TYR C 0.93 37.97791290283203 0.0
3DKF A X-ray 1.7999999523162842 Monomer [CL]A:2 0.086663105 1230, 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 77.48719024658203 0.0
1230 1230 TYR C 1.0 127.74114990234375 0.0
1257 1257 THR H 1.0 91.41764831542969 0.0
1289 1289 THR H 0.92 75.46898651123047 0.0
1349 1349 TYR E 0.89 114.5146484375 0.0
1356 1356 TYR C 0.93 36.58207321166992 0.0
3LQ8 A X-ray 2.0199999809265137 Monomer [88Z]A:1 0.1 1234, 1235, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 71.5329818725586 19.179012298583984
1234 1234 TYR C 0.97 47.55662155151367 0.0
1235 1235 TYR C 1.0 32.94573974609375 0.0
1236 1236 SER C 1.0 41.9254264831543 0.0
1257 1257 THR H 1.0 82.41502380371094 0.0
1289 1289 THR H 0.92 39.54050827026367 0.0
3A4P A X-ray 2.5399999618530273 Monomer [DFQ]A:1362 0.06355155 1230, 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 69.3565444946289 19.554859161376953
1230 1230 TYR C 1.0 71.19722747802734 36.36600112915039
1257 1257 THR H 1.0 89.32339477539062 0.0
1289 1289 THR C 0.92 42.208473205566406 0.0
1349 1349 TYR E 0.89 113.39069366455078 0.0
1356 1356 TYR C 0.93 25.159032821655273 0.0
3Q6W A X-ray 1.75 Monomer [Q6W]A:1 0.1 1230, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 64.14291381835938 25.203588485717773
1230 1230 TYR C 1.0 143.9617156982422 0.0
1236 1236 SER E 1.0 17.254085540771484 0.0
1257 1257 THR H 1.0 73.89083099365234 0.0
1289 1289 THR H 0.92 75.80030059814453 0.0
1R1W A X-ray 1.7999999523162842 Monomer A 0.0 1230, 1257, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 65.16956329345703 0.0
1230 1230 TYR C 1.0 126.99528503417969 0.0
1257 1257 THR H 1.0 61.4223518371582 0.0
1349 1349 TYR E 0.89 118.30599975585938 0.0
1356 1356 TYR C 0.93 34.5279426574707 0.0
3DKG A X-ray 1.909999966621399 Monomer [CL]A:2 0.08319675 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 64.42906951904297 0.0
1257 1257 THR H 1.0 88.75700378417969 0.0
1289 1289 THR H 0.92 80.4334716796875 0.0
1349 1349 TYR E 0.89 113.06143951416016 0.0
1356 1356 TYR C 0.93 85.22816467285156 0.0
5HO6 A X-ray 1.9700000286102295 Monomer [63K]A:1401 0.1 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 78.91427612304688 34.871917724609375
1257 1257 THR H 1.0 83.7370376586914 0.0
1289 1289 THR H 0.92 80.70621490478516 0.0
1349 1349 TYR E 0.89 113.4755859375 0.0
1356 1356 TYR C 0.93 67.02800750732422 0.0
4IWD A X-ray 1.9900000095367432 Monomer [1JC]A:1401 0.1 1230, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 60.25863265991211 0.0
1230 1230 TYR C 1.0 156.24847412109375 0.0
1236 1236 SER E 1.0 16.772647857666016 0.0
1257 1257 THR H 1.0 85.32310485839844 0.0
1289 1289 THR H 0.92 71.24165344238281 0.0
3QTI A X-ray 2.0 Monomer [CL]A:1361 0.09668805 1230, 1257, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 55.57985305786133 0.0
1230 1230 TYR C 1.0 72.71159362792969 0.0
1257 1257 THR H 1.0 86.95853424072266 0.0
1349 1349 TYR E 0.89 115.04622650146484 0.0
1356 1356 TYR C 0.93 38.84227752685547 0.0
5HOA A X-ray 2.140000104904175 Monomer [63K]A:1401 0.1 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 80.84355926513672 31.708057403564453
1257 1257 THR H 1.0 82.46916961669922 0.0
1289 1289 THR H 0.92 74.17512512207031 0.0
1349 1349 TYR E 0.89 115.0301284790039 0.0
1356 1356 TYR C 0.93 69.31710052490234 0.0
3C1X A X-ray 2.1700000762939453 Monomer [CKK]A:1500 0.1 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 60.65704345703125 8.768280029296875
1257 1257 THR H 1.0 83.58920288085938 0.0
1289 1289 THR C 0.92 73.78736877441406 0.0
1349 1349 TYR E 0.89 109.47221374511719 0.0
1356 1356 TYR C 0.93 38.948081970214844 0.0
5HOR A X-ray 2.200000047683716 Monomer [63K]A:1401 0.1 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 78.0802001953125 31.772903442382812
1257 1257 THR H 1.0 73.88414001464844 0.0
1289 1289 THR H 0.92 57.83264923095703 0.0
1349 1349 TYR E 0.89 112.41464233398438 0.0
1356 1356 TYR C 0.93 64.6858901977539 0.0
3R7O A X-ray 2.299999952316284 Monomer [M61]A:1 0.1 1230, 1236, 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 60.436763763427734 23.860233306884766
1230 1230 TYR C 1.0 153.64051818847656 0.0
1236 1236 SER E 1.0 12.254013061523438 0.0
1257 1257 THR H 1.0 80.05397033691406 0.0
1289 1289 THR H 0.92 69.12129211425781 0.0
3CTH A X-ray 2.299999952316284 Monomer A 0.0 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 64.15079498291016 0.0
1257 1257 THR C 1.0 71.83734130859375 0.0
1289 1289 THR C 0.92 74.98309326171875 0.0
1349 1349 TYR E 0.89 110.9891128540039 0.0
1356 1356 TYR C 0.93 51.86016082763672 0.0
3L8V A X-ray 2.4000000953674316 Monomer [L8V]A:1 0.1 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 58.97406005859375 3.851916790008545
1257 1257 THR C 1.0 85.83391571044922 0.0
1289 1289 THR H 0.92 70.95252227783203 0.0
1349 1349 TYR E 0.89 114.03502655029297 0.0
1356 1356 TYR C 0.93 48.26503372192383 0.0
3CE3 A X-ray 2.4000000953674316 Monomer [1FN]A:1401 0.1 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 69.36029052734375 7.381254196166992
1257 1257 THR H 1.0 86.88512420654297 0.0
1289 1289 THR H 0.92 58.42744827270508 0.0
1349 1349 TYR E 0.89 113.84444427490234 0.0
1356 1356 TYR C 0.93 68.98124694824219 0.0
3CTJ A X-ray 2.5 Monomer [320]A:2001 0.1 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 54.97572708129883 8.397923469543457
1257 1257 THR C 1.0 76.35484313964844 0.0
1289 1289 THR C 0.92 77.22325134277344 0.0
1349 1349 TYR E 0.89 121.17758178710938 0.0
1356 1356 TYR C 0.93 48.91748809814453 0.0
3F82 A X-ray 2.5 Monomer [353]A:2001 0.1 1257, 1289, 1349, 1356
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 69.73228454589844 6.446791172027588
1257 1257 THR H 1.0 75.95742797851562 0.0
1289 1289 THR H 0.92 86.62307739257812 0.0
1349 1349 TYR E 0.89 115.763916015625 0.0
1356 1356 TYR C 0.93 42.078067779541016 0.0
5T3Q A X-ray 2.0 2 A 0.72452855 1257, 1289, 1349
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 58.485618591308594 0.0
1257 1257 THR H 1.0 80.10395812988281 0.0
1289 1289 THR H 0.92 76.15921783447266 0.0
1349 1349 TYR C 0.89 25.675020217895508 0.0
3U6H A X-ray 2.0 2 A 0.6437068 1257, 1289, 1349
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 68.5322494506836 0.0
1257 1257 THR H 1.0 84.19017791748047 0.0
1289 1289 THR C 0.92 78.42198944091797 0.0
1349 1349 TYR C 0.89 27.748672485351562 0.0
3U6I A X-ray 2.0999999046325684 2 [044]A:1 0.6284073 1257, 1289, 1349
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 63.11156463623047 15.362921714782715
1257 1257 THR H 1.0 96.03498840332031 0.0
1289 1289 THR H 0.92 77.96760559082031 0.0
1349 1349 TYR C 0.89 26.699481964111328 0.0
3EFK A X-ray 2.200000047683716 2 B 1.0 1257, 1289, 1349
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 59.18517303466797 0.0
1257 1257 THR C 1.0 95.10205078125 0.0
1289 1289 THR C 0.92 84.98915100097656 0.0
1349 1349 TYR C 0.89 31.37242889404297 0.0
2RFN A X-ray 2.5 2 B 0.74259716 1257, 1289, 1349
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 70.69810485839844 0.0
1257 1257 THR H 1.0 82.9188461303711 0.0
1289 1289 THR C 0.92 82.4808578491211 0.0
1349 1349 TYR C 0.89 33.24301528930664 0.0
3EFJ A X-ray 2.5999999046325684 2 B 1.0 1257, 1289, 1349
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 71.41288757324219 0.0
1257 1257 THR C 1.0 97.13939666748047 0.0
1289 1289 THR C 0.92 80.31522369384766 0.0
1349 1349 TYR C 0.89 33.04701232910156 0.0
3Q6U A X-ray 1.600000023841858 Monomer A 0.0 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 61.03459930419922 0.0
1257 1257 THR H 1.0 74.5400619506836 0.0
1289 1289 THR H 0.92 70.59696197509766 0.0
4EEV A X-ray 1.7999999523162842 Monomer A 0.0 1257, 1289
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1159 1159 TYR C 1.0 67.17443084716797 0.0
1257 1257 THR H 1.0 76.25873565673828 0.0
1289 1289 THR C 0.92 82.59001922607422 0.0
3BUX A X-ray 1.350000023841858 2 B 1.0 1000
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
1000 1000 SER C 0.85 114.0623550415039 19.68642807006836
2UZX B X-ray 2.799999952316284 4 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
444 444 THR E 0.95 4.960783004760742 0.0
451 451 THR E 0.96 0.9185013771057129 0.0
4K3J B X-ray 2.799999952316284 2 A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
444 444 THR E 0.95 3.1777210235595703 0.0
451 451 THR E 0.96 1.4576246738433838 0.0
4O3T B X-ray 2.990000009536743 2 A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
444 444 THR E 0.95 3.0680079460144043 0.0
451 451 THR E 0.96 1.645250678062439 0.0
4O3U B X-ray 3.0399999618530273 2 A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
444 444 THR E 0.95 2.4434735774993896 0.0
451 451 THR E 0.96 1.848941445350647 0.0
1SHY B X-ray 3.2200000286102295 Monomer A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
444 444 THR E 0.95 3.614382743835449 0.0
451 451 THR E 0.96 0.585637629032135 0.0
2UZY B X-ray 4.0 2 A 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
444 444 THR E 0.95 2.32889723777771 0.0
451 451 THR E 0.96 0.24966563284397125 0.0

Mutations

Showing 28 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
143 R Q Polymorphism
150 H Y Polymorphism
156 S L Polymorphism
168 E D Polymorphism
238 L S Polymorphism
316 I M Polymorphism
320 A V Polymorphism
375 N K Unclassified
385 C Y Polymorphism
773 P L Unclassified Gastric cancer
841 F V Disease Deafness, autosomal recessive, 97 (DFNB97) [MIM:616705]
970 R C Polymorphism
991 P S Unclassified Gastric cancer
992 T I Polymorphism
1003 Y S Disease
1092 V I Disease Renal cell carcinoma papillary (RCCP) [MIM:605074]
1094 H L Disease Renal cell carcinoma papillary (RCCP) [MIM:605074]
1106 H D Disease Renal cell carcinoma papillary (RCCP) [MIM:605074]
1131 M T Disease Renal cell carcinoma papillary (RCCP) [MIM:605074]
1173 T I Disease Hepatocellular carcinoma (HCC) [MIM:114550]
1188 V L Disease Renal cell carcinoma papillary (RCCP) [MIM:605074]
1195 L V Disease Renal cell carcinoma papillary (RCCP) [MIM:605074]
1220 V I Disease Renal cell carcinoma papillary (RCCP) [MIM:605074]
1228 D N Disease Renal cell carcinoma papillary (RCCP) [MIM:605074]
1230 Y C Disease Renal cell carcinoma papillary (RCCP) [MIM:605074]
1244 K R Disease Hepatocellular carcinoma (HCC) [MIM:114550]
1250 M I Disease Hepatocellular carcinoma (HCC) [MIM:114550]
1294 V I Polymorphism