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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 7 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
9 SER UP, PRIDE Experimental yes
13 SER PRIDE yes
215 SER PRIDE
216 TYR UP, PRIDE Experimental
219 SER PRIDE
389 SER UP, PRIDE Similarity yes
390 THR UP, PRIDE Combined 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 11 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
9 7 27 3 11
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 14 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
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 -
PXD004415 2 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
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
PXD003531 2 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD006482 6 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 20 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 16 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD001374 1 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell -
PXD001550 4 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
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 -
9 7 15 3 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 8 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 1 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
13 7 27 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 -
PXD005366 4 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
215 206 220 10 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD005366 11 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 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
PXD001374 1 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell -
PXD003198 3 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
215 210 220 6 9
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 -
PXD001546 5 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
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 -
PXD001565 54 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD005366 44 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 24 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
PXD004452 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD003198 3 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
216 206 220 11 6
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 8 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
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
PXD004415 2 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD005366 11 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 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD003198 141 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
216 210 220 7 8
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 113 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000612 26 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 15 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD002286 4 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD005366 46 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 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD003198 317 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
219 206 220 14 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
219 210 220 10 8
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 2 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 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
PXD001546 5 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD003531 7 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 8 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 -
PXD003198 2 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
389 384 405 6 1
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
390 384 405 7 5
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 -
PXD000612 13 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 4 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 -
PXD002286 6 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -

Structures

Showing 75 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
1J1B A X-ray 1.7999999523162842 2 B 0.6483508 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 23.532690048217773 18.39882469177246
216 216 TYR C 1.0 172.3190155029297 165.9981689453125
219 219 SER C 1.0 31.203153610229492 27.626501083374023
1Q5K A X-ray 1.940000057220459 2 [TMU]A:901 0.1 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 21.844938278198242 0.0
216 216 TYR C 1.0 173.75540161132812 0.0
219 219 SER C 1.0 28.896549224853516 0.0
4PTE A X-ray 2.0299999713897705 2 B 1.0 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 24.012531280517578 20.207843780517578
216 216 TYR C 1.0 170.7549285888672 153.1782684326172
219 219 SER E 1.0 28.632556915283203 26.290647506713867
4NM3 A X-ray 2.0999999046325684 2 B 0.25211012 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 15.761117935180664 0.0
215 215 SER C 1.0 29.903079986572266 0.0
216 216 TYR C 1.0 146.18685913085938 0.0
219 219 SER C 1.0 24.89570426940918 0.0
1Q41 A X-ray 2.0999999046325684 2 B 0.94985497 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 24.18265724182129 10.9766845703125
216 216 TYR C 1.0 175.15621948242188 160.30062866210938
219 219 SER C 1.0 21.126131057739258 20.632606506347656
1J1C A X-ray 2.0999999046325684 2 B 0.3166759 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 22.77289581298828 17.301748275756836
216 216 TYR C 1.0 172.04562377929688 165.818603515625
219 219 SER C 1.0 31.633995056152344 28.10359764099121
3DU8 A X-ray 2.200000047683716 2 B 0.10932999 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 24.016023635864258 12.442216873168945
216 216 TYR C 1.0 171.85403442382812 142.6285400390625
219 219 SER C 1.0 29.81452178955078 26.566980361938477
1Q3D A X-ray 2.200000047683716 Monomer [STU]A:451 0.1 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 24.564176559448242 0.0
216 216 TYR C 1.0 173.663330078125 0.0
219 219 SER E 1.0 27.499216079711914 0.0
4ACC A X-ray 2.2100000381469727 2 B 1.0 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 24.99361801147461 20.10031509399414
216 216 TYR C 1.0 172.63880920410156 158.9847412109375
219 219 SER C 1.0 29.4179744720459 25.821758270263672
1R0E A X-ray 2.25 2 B 0.5338809 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 25.678081512451172 21.13410186767578
216 216 TYR C 1.0 173.0907440185547 159.97669982910156
219 219 SER E 1.0 29.491106033325195 27.654321670532227
3I4B A X-ray 2.299999952316284 2 B 0.89028835 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 26.156038284301758 18.850210189819336
216 216 TYR C 1.0 175.2129669189453 160.25804138183594
219 219 SER C 1.0 29.466035842895508 26.92691421508789
4NM7 A X-ray 2.299999952316284 3 C 0.25806874 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 25.024452209472656 0.0
216 216 TYR C 1.0 172.8389129638672 41.436405181884766
219 219 SER C 1.0 25.971601486206055 13.296663284301758
4NM5 A X-ray 2.299999952316284 6 C 0.2488602 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 19.830318450927734 0.0
216 216 TYR C 1.0 178.7855224609375 39.97431945800781
219 219 SER C 1.0 23.065338134765625 12.470963478088379
1Q3W A X-ray 2.299999952316284 2 B 0.67522556 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 27.7191104888916 11.215079307556152
216 216 TYR C 1.0 175.53721618652344 150.51197814941406
219 219 SER C 1.0 22.264631271362305 22.141510009765625
2JLD A X-ray 2.3499999046325684 2 [AG1]A:1385 0.57255274 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 24.176424026489258 0.0
216 216 TYR C 1.0 174.53817749023438 0.0
219 219 SER C 1.0 29.79070472717285 0.0
4PTG A X-ray 2.359999895095825 Monomer [2WG]A:501 0.1 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 22.21405029296875 0.0
216 216 TYR C 1.0 174.87210083007812 0.0
219 219 SER E 1.0 28.279869079589844 0.0
1PYX A X-ray 2.4000000953674316 2 [ANP]A:1001 0.021355156 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 27.05760383605957 0.0
216 216 TYR C 1.0 174.9050750732422 0.0
219 219 SER C 1.0 24.019817352294922 0.0
4NM0 A X-ray 2.5 2 B 0.21194741 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 26.0909366607666 5.7671637535095215
216 216 TYR C 1.0 84.31012725830078 2.842622995376587
219 219 SER C 1.0 34.53782653808594 0.0
5F94 A X-ray 2.509999990463257 2 B 0.111076035 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 20.84792709350586 17.65662956237793
216 216 TYR C 1.0 167.72897338867188 153.5906524658203
219 219 SER C 1.0 28.863637924194336 26.35063934326172
5F95 A X-ray 2.5199999809265137 Monomer [3UP]A:401 0.1 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 21.990907669067383 0.0
216 216 TYR C 1.0 172.7266387939453 0.0
219 219 SER E 1.0 28.49927520751953 0.0
4ACD A X-ray 2.5999999046325684 2 B 0.95134056 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 23.887239456176758 19.249643325805664
216 216 TYR C 1.0 178.62049865722656 159.9365997314453
219 219 SER C 1.0 27.931100845336914 25.19948387145996
4ACH A X-ray 2.5999999046325684 2 B 0.7436806 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 21.75130271911621 17.02254867553711
216 216 TYR C 1.0 176.0126495361328 162.53131103515625
219 219 SER C 1.0 34.229190826416016 30.142465591430664
4ACG A X-ray 2.5999999046325684 2 B 0.5522475 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 20.498035430908203 16.25356101989746
216 216 TYR C 1.0 174.93614196777344 161.4231719970703
219 219 SER C 1.0 30.828481674194336 28.40248680114746
3SD0 A X-ray 2.700000047683716 Monomer [TSK]A:400 0.20016117 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 26.17961311340332 0.0
216 216 TYR C 1.0 164.74755859375 0.0
219 219 SER C 1.0 37.29789733886719 0.0
3Q3B A X-ray 2.700000047683716 2 [55E]A:421 0.1 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 28.668472290039062 0.0
216 216 TYR C 1.0 171.8158416748047 0.0
219 219 SER C 1.0 21.145484924316406 0.0
1I09 A X-ray 2.700000047683716 2 [PO4]A:421 0.05224653 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 20.121034622192383 0.0
216 216 TYR C 1.0 161.06712341308594 0.0
219 219 SER C 1.0 21.73491859436035 0.0
4PTC A X-ray 2.7100000381469727 2 B 0.6664191 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 22.774417877197266 20.265714645385742
216 216 TYR C 1.0 179.930908203125 151.7694549560547
219 219 SER E 1.0 36.70244598388672 30.328096389770508
4B7T A X-ray 2.7699999809265137 2 B 0.7685635 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 29.880809783935547 0.0
216 216 TYR C 1.0 167.33045959472656 0.0
219 219 SER C 1.0 29.2016658782959 0.0
1Q4L A X-ray 2.7699999809265137 2 [679]A:451 0.1 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 21.31957244873047 0.0
216 216 TYR C 1.0 174.32232666015625 0.0
219 219 SER C 1.0 34.12773513793945 0.0
1UV5 A X-ray 2.799999952316284 2 [CO]A:1386 0.19058801 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 20.51606559753418 0.0
216 216 TYR C 1.0 165.72117614746094 0.0
219 219 SER C 1.0 34.28633117675781 0.0
1H8F A X-ray 2.799999952316284 Monomer B 0.0 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 29.325725555419922 23.827207565307617
216 216 TYR C 1.0 175.23191833496094 161.11270141601562
219 219 SER C 1.0 21.20897674560547 21.085336685180664
3L1S A X-ray 2.9000000953674316 Monomer [Z92]A:421 0.1 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 26.673412322998047 0.0
216 216 TYR C 1.0 175.81307983398438 0.0
219 219 SER C 1.0 30.492765426635742 0.0
3PUP A X-ray 2.990000009536743 2 [OS1]A:421 0.57296747 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 24.60275650024414 0.0
216 216 TYR C 1.0 172.480712890625 0.0
219 219 SER E 1.0 29.19281005859375 0.0
4IQ6 A X-ray 3.119999885559082 2 [IQ6]A:501 0.1 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 25.215984344482422 0.0
216 216 TYR C 1.0 174.33859252929688 0.0
219 219 SER E 1.0 37.23467254638672 0.0
3M1S A X-ray 3.130000114440918 2 B 1.0 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 23.950395584106445 17.652122497558594
216 216 TYR C 1.0 175.97438049316406 150.51522827148438
219 219 SER E 1.0 31.564897537231445 28.22188949584961
2O5K A X-ray 3.200000047683716 Monomer [HBM]A:0 0.1 215, 216, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 54.066925048828125 0.0
216 216 TYR C 1.0 154.86013793945312 0.0
219 219 SER C 1.0 15.24100112915039 0.0
4AFJ A X-ray 1.9800000190734863 8 X 0.37412518 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 27.62842559814453 0.0
219 219 SER C 1.0 32.28833770751953 0.0
5K5N A X-ray 2.200000047683716 Monomer [SO4]A:4002 0.078384474 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 28.0147762298584 0.0
219 219 SER C 1.0 30.35230255126953 0.0
3SAY A X-ray 2.2300000190734863 Monomer [MLA]A:432 0.063997105 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 30.428592681884766 0.0
219 219 SER C 1.0 32.95795440673828 0.0
4J71 A X-ray 2.309999942779541 2 [SO4]A:502 0.034611247 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 19.5611629486084 0.0
219 219 SER C 1.0 35.94215393066406 0.0
3ZRK A X-ray 2.369999885559082 8 X 0.34716082 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 29.669109344482422 0.0
219 219 SER C 1.0 30.720491409301758 0.0
3F7Z A X-ray 2.4000000953674316 Monomer B 0.0 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 19.64811134338379 0.0
219 219 SER C 1.0 37.5105094909668 0.0
3GB2 A X-ray 2.4000000953674316 Monomer [G3B]A:999 0.1 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 23.932239532470703 0.0
219 219 SER C 1.0 35.90624237060547 0.0
5KPK A X-ray 2.4000000953674316 Monomer [6VK]A:500 0.1 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 25.79889488220215 0.0
219 219 SER C 1.0 31.143909454345703 0.0
1O9U A X-ray 2.4000000953674316 2 B 1.0 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 32.063438415527344 0.0
219 219 SER C 1.0 24.648584365844727 0.0
5HLP A X-ray 2.450000047683716 Monomer [65A]A:501 0.1 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 26.21132469177246 0.0
219 219 SER C 1.0 33.35786437988281 0.0
3ZRL A X-ray 2.4800000190734863 8 X 0.31498086 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 30.589298248291016 0.0
219 219 SER C 1.0 29.36543083190918 0.0
3ZRM A X-ray 2.490000009536743 8 X 0.3789366 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 30.07267189025879 0.0
219 219 SER C 1.0 30.19568634033203 0.0
3F88 A X-ray 2.5999999046325684 Monomer [3HT]A:999 0.08055695 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 23.012948989868164 0.0
219 219 SER C 1.0 31.890134811401367 0.0
6B8J A X-ray 2.5999999046325684 2 C 0.52715605 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 18.99122428894043 0.0
219 219 SER C 1.0 33.31909942626953 0.0
5KPL A X-ray 2.5999999046325684 Monomer [6VL]A:500 0.1 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 23.840415954589844 0.0
219 219 SER C 1.0 35.3239631652832 0.0
1GNG A X-ray 2.5999999046325684 4 X 0.41614953 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 25.88688850402832 0.0
219 219 SER C 1.0 30.64275550842285 0.0
3ZDI A X-ray 2.640000104904175 2 B 0.4710366 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 28.135356903076172 0.0
219 219 SER C 1.0 35.3741569519043 0.0
5KPM A X-ray 2.690000057220459 Monomer [6VM]A:500 0.1 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 19.188140869140625 0.0
219 219 SER C 1.0 30.60563087463379 0.0
4J1R A X-ray 2.700000047683716 2 [K]A:503 0.084203616 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 19.50405502319336 0.0
219 219 SER C 1.0 28.959131240844727 0.0
2OW3 A X-ray 2.799999952316284 Monomer [BIM]A:387 0.1 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 31.02378273010254 0.0
219 219 SER C 1.0 39.529518127441406 0.0
5T31 A X-ray 2.8499999046325684 Monomer [75F]A:501 0.1 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 23.940847396850586 0.0
219 219 SER C 1.0 32.13833999633789 0.0
5HLN A X-ray 3.0999999046325684 2 B 0.5381006 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 16.381824493408203 13.111578941345215
219 219 SER C 1.0 33.67170333862305 0.0
5OY4 A X-ray 3.200000047683716 4 X 0.4460143 215, 219
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 29.015857696533203 0.0
219 219 SER C 1.0 29.598974227905273 0.0
1O6L C X-ray 1.600000023841858 2 A 0.34782803 9
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 131.03488159179688 47.34870147705078
9 9 SER C 0.75 113.10028076171875 63.71498489379883
1O6K C X-ray 1.7000000476837158 2 A 0.34467694 9
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 131.04495239257812 58.79274368286133
9 9 SER C 0.75 111.95362854003906 65.53472900390625
2JDO C X-ray 1.7999999523162842 2 A 0.6551418 9
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 125.40179443359375 20.94764518737793
9 9 SER C 0.75 110.77764892578125 64.30216217041016
2X39 C X-ray 1.9299999475479126 2 A 0.52367955 9
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 124.62056732177734 19.424575805664062
9 9 SER C 0.75 111.24041748046875 66.0466079711914
2UW9 C X-ray 2.0999999046325684 2 A 0.6926176 9
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 127.90852355957031 41.693538665771484
9 9 SER C 0.75 111.13191223144531 64.80335235595703
3E87 C X-ray 2.299999952316284 2 A 1.0 9
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 122.56932067871094 20.09380340576172
9 9 SER C 0.75 119.10684204101562 62.717559814453125
2JDR C X-ray 2.299999952316284 2 A 0.8581733 9
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 131.80311584472656 55.16480255126953
9 9 SER C 0.75 118.27754211425781 84.62224578857422
3E88 C X-ray 2.5 2 A 1.0 9
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 123.63052368164062 25.3900203704834
9 9 SER C 0.75 119.53727722167969 76.03838348388672
4DIT A X-ray 2.5999999046325684 Monomer [0KD]A:501 0.1 215
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
215 215 SER C 1.0 57.04362487792969 0.0
3E8D C X-ray 2.700000047683716 2 A 0.96207273 9
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 116.48987579345703 17.24844741821289
9 9 SER C 0.75 119.05621337890625 74.39259338378906
2XH5 C X-ray 2.7200000286102295 2 A 0.9402706 9
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 THR C 0.91 125.44255828857422 18.971323013305664
9 9 SER C 0.75 113.57527923583984 66.31871795654297
3CQW C X-ray 2.0 2 A 0.53416586
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 6 THR C 0.91 126.3104019165039 20.686908721923828
9 7 SER C 0.75 112.39225006103516 67.47065734863281
3CQU C X-ray 2.200000047683716 2 A 0.9542653
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 6 THR C 0.91 123.47635650634766 36.021060943603516
9 7 SER C 0.75 114.65403747558594 94.6681900024414
3QKK C X-ray 2.299999952316284 2 A 0.39465916
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 6 THR C 0.91 123.1143798828125 18.395835876464844
9 7 SER C 0.75 120.36078643798828 62.18935775756836
3MV5 C X-ray 2.4700000286102295 2 A 0.71074307
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 6 THR C 0.91 122.96875762939453 24.598236083984375
9 7 SER C 0.75 114.2384262084961 76.32333374023438
4EKK C X-ray 2.799999952316284 2 A 0.3433753
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 6 THR C 0.91 125.95808410644531 34.11312484741211
9 7 SER C 0.75 108.2776870727539 60.180076599121094

Mutations

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Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease