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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 11 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
103 SER UP Combined
137 SER UP Experimental
210 THR UP, PRIDE Combined yes
214 THR UP, PRIDE Combined yes
269 SER UP Similarity
331 SER PRIDE yes
335 SER UP, PRIDE Experimental yes
375 SER UP Combined
383 SER PRIDE yes
450 SER UP, PRIDE Combined yes
498 THR UP Combined

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 12 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
210 208 225 3 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 2 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD004452 8 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
PXD000680 5 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
210 209 225 2 2
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 -
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
210 210 225 1 6
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 116 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 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 -
PXD001333 10 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 - -
PXD004452 10 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
214 208 225 7 4
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 -
PXD004415 2 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
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
PXD004452 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
214 209 225 6 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
214 210 225 5 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 79 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 -
331 325 345 7 2
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 -
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
331 325 338 7 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
331 325 337 7 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
335 325 345 11 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
383 365 388 19 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 7 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
450 442 456 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 23 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture

Structures

Showing 60 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
2YAC A X-ray 2.200000047683716 2 [ZN]A:502 0.34371114 103, 137, 210, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 56.38821792602539 0.0
137 137 SER E 1.0 4.785065650939941 0.0
210 210 THR C 1.0 108.77399444580078 0.0
214 214 THR C 1.0 109.7535629272461 0.0
217 217 TYR C 1.0 17.016786575317383 0.0
269 269 SER C 0.79 86.66265106201172 0.0
2V5Q A X-ray 2.299999952316284 2 D 1.0 103, 137, 210, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 52.254859924316406 0.0
137 137 SER E 1.0 5.871953010559082 1.2285045385360718
210 210 THR C 1.0 104.48006439208984 0.0
214 214 THR C 1.0 104.16204071044922 0.0
217 217 TYR C 1.0 37.16827392578125 0.0
269 269 SER C 0.79 81.4639663696289 0.0
4A4L A X-ray 2.3499999046325684 2 [ZN]A:1329 0.33247885 103, 137, 210, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 43.43751907348633 0.0
137 137 SER E 1.0 5.312450408935547 0.0
210 210 THR C 1.0 108.6332015991211 0.0
214 214 THR C 1.0 110.57076263427734 0.0
217 217 TYR C 1.0 18.85129737854004 0.0
269 269 SER C 0.79 85.57096099853516 0.0
3KB7 A X-ray 2.5 2 [ZN]A:346 0.33236825 103, 137, 210, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 42.58911895751953 0.0
137 137 SER E 1.0 5.082012176513672 0.0
210 210 THR C 1.0 111.60556030273438 0.0
214 214 THR C 1.0 112.84127044677734 0.0
217 217 TYR C 1.0 15.43999195098877 0.0
269 269 SER C 0.79 80.87752532958984 0.0
4A4O A X-ray 2.700000047683716 2 [ZN]A:1330 0.32409272 103, 137, 210, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 56.16826629638672 0.0
137 137 SER E 1.0 4.733410358428955 0.0
210 210 THR C 1.0 109.52098083496094 0.0
214 214 THR C 1.0 92.7128677368164 0.0
217 217 TYR C 1.0 21.069040298461914 0.0
269 269 SER C 0.79 82.9383316040039 0.0
4X9R A X-ray 1.399999976158142 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 70.04996490478516 0.0
383 383 SER H 0.63 47.255462646484375 0.0
387 387 SER C 0.71 33.92725372314453 0.0
445 445 TYR C 0.93 17.042144775390625 0.0
450 450 SER E 1.0 29.313810348510742 0.0
498 498 THR C 0.95 113.63646697998047 0.0
3P34 A X-ray 1.399999976158142 2 B 0.39375812 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 57.558223724365234 0.0
383 383 SER H 0.63 47.094139099121094 0.0
387 387 SER C 0.71 35.8809928894043 0.0
445 445 TYR C 0.93 62.489871978759766 0.0
450 450 SER E 1.0 29.52281951904297 0.0
498 498 THR C 0.95 115.14311981201172 0.0
3Q1I A X-ray 1.399999976158142 2 E 0.84447104 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 50.37166213989258 0.0
383 383 SER H 0.63 49.324337005615234 0.0
387 387 SER C 0.71 19.520849227905273 0.0
445 445 TYR C 0.93 96.80802917480469 0.0
450 450 SER E 1.0 38.06489944458008 0.0
498 498 THR C 0.95 119.46031188964844 0.0
4X9V A X-ray 1.4299999475479126 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 49.661376953125 0.0
383 383 SER H 0.63 48.29914093017578 0.0
387 387 SER C 0.71 16.740026473999023 0.0
445 445 TYR C 0.93 52.481510162353516 0.0
450 450 SER E 1.0 38.48231887817383 0.0
498 498 THR C 0.95 164.7071075439453 0.0
4O6W A X-ray 1.4500000476837158 2 C 0.9221612 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 61.674171447753906 0.0
383 383 SER H 0.63 36.530914306640625 0.0
387 387 SER C 0.71 21.032052993774414 0.0
445 445 TYR C 0.93 51.307228088378906 0.0
450 450 SER E 1.0 37.826622009277344 0.0
498 498 THR C 0.95 111.60232543945312 0.0
4DFW A X-ray 1.5499999523162842 2 D 0.4161731 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 72.37928009033203 0.0
383 383 SER H 0.63 53.430328369140625 0.0
387 387 SER C 0.71 33.53026580810547 0.0
445 445 TYR C 0.93 48.2365837097168 0.0
450 450 SER E 1.0 35.714385986328125 0.0
498 498 THR C 0.95 109.1611557006836 0.0
4LKL A X-ray 1.5800000429153442 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 76.2591781616211 0.0
383 383 SER H 0.63 42.045536041259766 0.0
387 387 SER C 0.71 35.37187576293945 0.0
445 445 TYR C 0.93 63.428184509277344 0.0
450 450 SER E 1.0 35.818687438964844 0.0
498 498 THR C 0.95 118.41400909423828 0.0
3FVH A X-ray 1.5800000429153442 2 B 0.9782746 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 22.766571044921875 0.0
383 383 SER H 0.63 48.47776412963867 0.0
387 387 SER C 0.71 31.235736846923828 0.0
445 445 TYR C 0.93 76.48050689697266 0.0
450 450 SER E 1.0 38.04457473754883 0.0
498 498 THR C 0.95 114.84725952148438 0.0
3P36 A X-ray 1.590000033378601 2 B 0.5828844 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 54.86555480957031 0.0
383 383 SER H 0.63 39.795658111572266 0.0
387 387 SER C 0.71 37.54325485229492 0.0
445 445 TYR C 0.93 60.4374885559082 0.0
450 450 SER E 1.0 11.390381813049316 0.0
498 498 THR C 0.95 123.58343505859375 0.0
4RCP A X-ray 1.600000023841858 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 63.07786560058594 0.0
383 383 SER H 0.63 51.52043533325195 0.0
387 387 SER C 0.71 30.675609588623047 0.0
445 445 TYR C 0.93 78.2227554321289 0.0
450 450 SER E 1.0 35.199764251708984 0.0
498 498 THR C 0.95 111.3946762084961 0.0
3P2W A X-ray 1.659999966621399 Monomer [SO4]A:596 0.045343634 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 42.75313949584961 0.0
383 383 SER H 0.63 51.797096252441406 0.0
387 387 SER C 0.71 36.481178283691406 0.0
445 445 TYR C 0.93 57.11678695678711 0.0
450 450 SER E 1.0 38.212989807128906 0.0
498 498 THR C 0.95 105.86975860595703 0.0
4O9W A X-ray 1.690000057220459 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 66.92822265625 0.0
383 383 SER H 0.63 44.14482879638672 0.0
387 387 SER C 0.71 42.3773078918457 0.0
445 445 TYR C 0.93 63.36148452758789 0.0
450 450 SER E 1.0 36.11799621582031 0.0
498 498 THR C 0.95 158.931640625 0.0
3HIH A X-ray 1.7000000476837158 2 [SO4]A:3 0.030996135 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 56.85094451904297 0.0
383 383 SER H 0.63 50.46796798706055 0.0
387 387 SER C 0.71 34.29652786254883 0.0
445 445 TYR C 0.93 54.24479675292969 0.0
450 450 SER E 1.0 37.0591926574707 0.0
498 498 THR C 0.95 115.84192657470703 0.0
4E9C A X-ray 1.7000000476837158 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 65.94375610351562 0.0
383 383 SER H 0.63 47.8150634765625 0.0
387 387 SER C 0.71 35.23064422607422 0.0
445 445 TYR C 0.93 58.368717193603516 0.0
450 450 SER E 1.0 25.734128952026367 0.0
498 498 THR C 0.95 114.68463134765625 0.0
3HIK A X-ray 1.7699999809265137 2 [GOL]A:2 0.8607912 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 55.4581413269043 0.0
383 383 SER H 0.63 35.681922912597656 0.0
387 387 SER C 0.71 33.30537033081055 0.0
445 445 TYR C 0.93 55.755577087402344 0.0
450 450 SER E 1.0 36.77469253540039 0.0
498 498 THR C 0.95 115.6136474609375 0.0
5NN1 A X-ray 1.7799999713897705 Monomer A 0.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 36.64279556274414 0.0
383 383 SER H 0.63 48.581581115722656 0.0
387 387 SER C 0.71 33.99699783325195 0.0
445 445 TYR C 0.93 59.71580123901367 0.0
450 450 SER E 1.0 36.785884857177734 0.0
498 498 THR C 0.95 160.5543670654297 0.0
3P2Z A X-ray 1.7899999618530273 2 B 0.7584072 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 46.91764831542969 0.0
383 383 SER H 0.63 66.07575988769531 0.0
445 445 TYR C 0.93 91.17616271972656 0.0
450 450 SER E 1.0 33.6557502746582 0.0
498 498 THR C 0.95 80.2808609008789 0.0
4O56 A X-ray 1.7999999523162842 2 B 0.43071437 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 56.059051513671875 0.0
383 383 SER H 0.63 39.18107986450195 0.0
387 387 SER C 0.71 33.49556350708008 0.0
445 445 TYR C 0.93 61.15380096435547 0.0
450 450 SER E 1.0 37.909088134765625 0.0
498 498 THR C 0.95 117.97466278076172 0.0
4WHK A X-ray 1.7999999523162842 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 63.97438049316406 0.0
383 383 SER H 0.63 57.9167594909668 0.0
387 387 SER C 0.71 37.107994079589844 0.0
445 445 TYR C 0.93 38.100467681884766 0.0
450 450 SER E 1.0 35.216796875 0.0
498 498 THR C 0.95 113.4208755493164 0.0
4X9W A X-ray 1.7999999523162842 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 49.82598114013672 0.0
383 383 SER H 0.63 47.743106842041016 0.0
387 387 SER C 0.71 41.80872344970703 0.0
445 445 TYR C 0.93 9.588153839111328 0.0
450 450 SER E 1.0 28.205747604370117 0.0
498 498 THR C 0.95 99.94290161132812 0.0
5NN2 A X-ray 1.809999942779541 Monomer [Z24]A:601 0.1 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 55.168270111083984 0.0
383 383 SER H 0.63 44.21522903442383 0.0
387 387 SER C 0.71 30.607463836669922 0.0
445 445 TYR C 0.93 62.954376220703125 0.0
450 450 SER E 1.0 38.10147476196289 0.0
498 498 THR C 0.95 158.25511169433594 0.0
5NFU A X-ray 1.809999942779541 2 C 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 56.6674690246582 0.0
383 383 SER H 0.63 50.91018295288086 0.0
387 387 SER C 0.71 35.96518325805664 0.0
445 445 TYR C 0.93 53.790435791015625 0.0
450 450 SER E 1.0 39.055320739746094 0.0
498 498 THR C 0.95 114.32933044433594 0.0
1UMW A X-ray 1.899999976158142 2 E 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 68.87779235839844 0.0
383 383 SER H 0.63 49.289337158203125 0.0
387 387 SER C 0.71 31.048980712890625 0.0
445 445 TYR C 0.93 43.30327224731445 0.0
450 450 SER E 1.0 38.69084167480469 0.0
498 498 THR C 0.95 108.94436645507812 0.0
4H71 A X-ray 1.9299999475479126 Monomer [PXE]A:702 0.064604394 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 50.17620849609375 0.0
383 383 SER H 0.63 49.250423431396484 0.0
387 387 SER C 0.71 37.28180694580078 0.0
445 445 TYR C 0.93 50.54231643676758 0.0
450 450 SER E 1.0 36.67737579345703 0.0
498 498 THR C 0.95 115.06124877929688 0.0
4H5X A X-ray 1.9500000476837158 Monomer [GOL]A:701 0.1 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 62.14645767211914 0.0
383 383 SER H 0.63 53.24932861328125 0.0
387 387 SER C 0.71 36.65431213378906 0.0
445 445 TYR C 0.93 52.60047149658203 0.0
450 450 SER E 1.0 35.91635513305664 0.0
498 498 THR C 0.95 110.84667205810547 0.0
2RKU A X-ray 1.9500000476837158 2 [ZN]A:501 0.344931 103, 137, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 55.13788604736328 0.0
137 137 SER E 1.0 5.012495040893555 0.0
214 214 THR C 1.0 94.9442138671875 0.0
217 217 TYR C 1.0 19.02587127685547 0.0
269 269 SER C 0.79 85.96282958984375 0.0
330 330 SER C 0.84 167.03053283691406 0.0
5NJE A X-ray 1.9800000190734863 Monomer A 0.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 55.47604751586914 0.0
383 383 SER H 0.63 46.21421813964844 0.0
387 387 SER C 0.71 35.89229965209961 0.0
445 445 TYR C 0.93 58.29376220703125 0.0
450 450 SER E 1.0 27.198766708374023 0.0
498 498 THR C 0.95 165.77598571777344 0.0
4LKM A X-ray 2.0 2 [SO4]A:701 0.6250227 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 60.978271484375 0.0
383 383 SER H 0.63 42.39646530151367 0.0
387 387 SER C 0.71 35.69173049926758 0.0
445 445 TYR C 0.93 48.70430374145508 0.0
450 450 SER E 1.0 34.84617614746094 0.0
498 498 THR C 0.95 114.4959716796875 0.0
4HY2 A X-ray 2.0 2 D 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 65.34516143798828 0.0
383 383 SER H 0.63 46.17219924926758 0.0
387 387 SER C 0.71 39.710693359375 0.0
445 445 TYR C 0.93 63.1627082824707 0.0
450 450 SER E 1.0 37.1104850769043 0.0
498 498 THR C 0.95 118.8941421508789 0.0
5J19 A X-ray 2.0 2 D 0.89640754 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 50.28417205810547 0.0
383 383 SER H 0.63 50.43474197387695 0.0
387 387 SER C 0.71 50.40512466430664 0.0
445 445 TYR C 0.93 62.24591064453125 0.0
450 450 SER E 1.0 37.70386505126953 0.0
498 498 THR C 0.95 116.2481689453125 0.0
5NMM A X-ray 2.0199999809265137 Monomer A 0.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 55.54182052612305 0.0
383 383 SER H 0.63 49.2745246887207 0.0
387 387 SER C 0.71 24.877742767333984 0.0
445 445 TYR C 0.93 59.451358795166016 0.0
450 450 SER E 1.0 40.193077087402344 0.0
498 498 THR C 0.95 158.0567626953125 0.0
3P35 A X-ray 2.0899999141693115 2 D 0.7320045 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 69.48159790039062 0.0
383 383 SER H 0.63 48.675819396972656 0.0
387 387 SER C 0.71 36.313724517822266 0.0
445 445 TYR C 0.93 73.86187744140625 0.0
450 450 SER E 1.0 26.86844253540039 0.0
498 498 THR C 0.95 109.57975769042969 0.0
3BZI A X-ray 2.0999999046325684 2 E 0.9341965 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 55.18738555908203 0.0
383 383 SER H 0.63 34.21381759643555 0.0
387 387 SER C 0.71 34.99640655517578 0.0
445 445 TYR C 0.93 56.30323028564453 0.0
450 450 SER E 1.0 36.574886322021484 0.0
498 498 THR C 0.95 108.95970916748047 0.0
2OWB A X-ray 2.0999999046325684 2 [ZN]A:501 0.32982877 103, 137, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 52.23332595825195 0.0
137 137 SER E 1.0 4.780202865600586 0.0
214 214 THR C 1.0 96.88264465332031 0.0
217 217 TYR C 1.0 21.446897506713867 0.0
269 269 SER C 0.79 85.4898452758789 0.0
330 330 SER C 0.84 165.01287841796875 0.0
4E67 A X-ray 2.0999999046325684 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 70.29117584228516 0.0
383 383 SER H 0.63 51.993553161621094 0.0
387 387 SER C 0.71 16.2156982421875 0.0
445 445 TYR C 0.93 61.41969680786133 0.0
450 450 SER E 1.0 35.60098648071289 0.0
498 498 THR C 0.95 106.00849914550781 0.0
4J52 A X-ray 2.299999952316284 2 [ZN]A:401 0.44351095 103, 137, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 48.25313949584961 0.0
137 137 SER E 1.0 3.738370895385742 0.0
214 214 THR C 1.0 95.58427429199219 0.0
217 217 TYR C 1.0 17.974788665771484 0.0
269 269 SER C 0.79 85.98548126220703 0.0
330 330 SER C 0.84 167.07278442382812 0.0
1Q4K A X-ray 2.299999952316284 2 D 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 56.8025016784668 0.0
383 383 SER H 0.63 45.22255325317383 0.0
387 387 SER C 0.71 34.54903030395508 0.0
445 445 TYR C 0.93 73.20849609375 0.0
450 450 SER E 1.0 32.475460052490234 0.0
498 498 THR C 0.95 112.90909576416016 0.0
3C5L A X-ray 2.3299999237060547 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 74.9518051147461 0.0
383 383 SER H 0.63 48.465538024902344 0.0
387 387 SER C 0.71 29.383779525756836 0.0
445 445 TYR C 0.93 31.043386459350586 0.0
450 450 SER E 1.0 38.47438049316406 0.0
498 498 THR C 0.95 115.83521270751953 0.0
3P37 A X-ray 2.380000114440918 2 E 0.9788775 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 42.729122161865234 0.0
383 383 SER H 0.63 42.491363525390625 0.0
387 387 SER C 0.71 36.8134880065918 0.0
445 445 TYR C 0.93 57.93388366699219 0.0
450 450 SER E 1.0 37.056880950927734 0.0
498 498 THR C 0.95 110.86502838134766 0.0
2OU7 A X-ray 2.4000000953674316 2 [ZN]A:501 0.2510268 103, 137, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 54.09498596191406 0.0
137 137 SER E 1.0 5.233815670013428 0.0
214 214 THR C 1.0 90.52405548095703 0.0
217 217 TYR C 1.0 22.786306381225586 0.0
269 269 SER C 0.79 80.86116790771484 0.0
3FC2 A X-ray 2.450000047683716 2 [ZN]A:8 0.3536162 103, 137, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 45.030548095703125 0.0
137 137 SER E 1.0 4.7804036140441895 0.0
214 214 THR C 1.0 92.0544204711914 0.0
217 217 TYR C 1.0 16.983644485473633 0.0
269 269 SER C 0.79 82.70864868164062 0.0
4J53 A X-ray 2.5 2 [ZN]A:401 0.47417068 103, 137, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 48.20470428466797 0.0
137 137 SER E 1.0 4.763315200805664 0.0
214 214 THR C 1.0 96.70867919921875 0.0
217 217 TYR C 1.0 20.93636703491211 0.0
269 269 SER C 0.79 85.70938873291016 0.0
330 330 SER C 0.84 164.24200439453125 0.0
3THB A X-ray 2.5 2 [ZN]A:502 0.36599642 103, 137, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 45.539764404296875 0.0
137 137 SER E 1.0 4.079411506652832 0.0
214 214 THR C 1.0 110.44841003417969 0.0
217 217 TYR C 1.0 23.856760025024414 0.0
269 269 SER C 0.79 86.86288452148438 0.0
5TA6 A X-ray 2.5 2 [ZN]A:1001 0.46710283 103, 137, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 46.2193489074707 0.0
137 137 SER E 1.0 3.3371658325195312 0.0
214 214 THR C 1.0 105.67228698730469 0.0
217 217 TYR C 1.0 20.05278205871582 0.0
269 269 SER C 0.79 82.35763549804688 0.0
330 330 SER C 0.84 168.5543975830078 0.0
5TA8 A X-ray 2.5999999046325684 2 [ZN]A:401 0.42279854 103, 137, 214, 269
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
103 103 SER H 0.66 46.28388977050781 0.0
137 137 SER E 1.0 3.6563947200775146 0.0
214 214 THR C 1.0 96.95244598388672 0.0
217 217 TYR C 1.0 18.03114128112793 0.0
269 269 SER C 0.79 82.8535385131836 0.0
330 330 SER C 0.84 166.7088623046875 0.0
4HAB A X-ray 2.6500000953674316 Monomer D 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 53.99542236328125 0.0
383 383 SER H 0.63 49.98112106323242 0.0
387 387 SER C 0.71 35.66654968261719 0.0
445 445 TYR C 0.93 61.57229995727539 0.0
450 450 SER E 1.0 44.08200454711914 0.0
498 498 THR C 0.95 103.39408874511719 0.0
5NEI A X-ray 2.680000066757202 Monomer [8VB]A:701 0.1 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER C 0.41 61.67439651489258 0.0
383 383 SER H 0.63 49.32583999633789 0.0
387 387 SER H 0.71 38.40849685668945 0.0
445 445 TYR C 0.93 50.74070739746094 0.0
450 450 SER E 1.0 37.336910247802734 0.0
498 498 THR C 0.95 178.71498107910156 0.0
4WHL A X-ray 2.7100000381469727 2 B 1.0 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 66.71793365478516 0.0
383 383 SER H 0.63 40.36495590209961 0.0
387 387 SER C 0.71 36.04363250732422 0.0
445 445 TYR C 0.93 63.164337158203125 0.0
450 450 SER E 1.0 33.34421157836914 0.0
498 498 THR C 0.95 172.22689819335938 0.0
4E9D A X-ray 2.75 2 E 0.6691361 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER C 0.41 62.23662185668945 0.0
383 383 SER H 0.63 53.58794021606445 0.0
387 387 SER C 0.71 37.73656463623047 0.0
445 445 TYR C 0.93 43.417545318603516 0.0
450 450 SER E 1.0 38.621910095214844 0.0
498 498 THR C 0.95 105.52857971191406 0.0
4HCO A X-ray 2.75 Monomer [IMW]A:702 0.05701685 375, 383, 450, 498
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 70.8488540649414 0.0
383 383 SER H 0.63 54.02787780761719 0.0
387 387 SER C 0.71 41.11347579956055 0.0
445 445 TYR C 0.93 52.509334564208984 0.0
450 450 SER E 1.0 40.627254486083984 0.0
498 498 THR C 0.95 109.75626373291016 0.0
3RQ7 A X-ray 1.5499999523162842 2 B 0.95540303 375, 383, 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 62.94528579711914 0.0
383 383 SER H 0.63 48.76597595214844 0.0
387 387 SER C 0.71 17.419509887695312 0.0
445 445 TYR C 0.93 61.95956802368164 0.0
450 450 SER E 1.0 37.75624465942383 0.0
4WHH A X-ray 1.899999976158142 2 [SO4]A:701 0.40431917 375, 383, 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 63.99027633666992 0.0
383 383 SER H 0.63 45.64794921875 0.0
387 387 SER C 0.71 39.071189880371094 0.0
445 445 TYR C 0.93 59.570716857910156 0.0
450 450 SER E 1.0 36.83322525024414 0.0
2OGQ A X-ray 1.9500000476837158 Monomer A 0.0 375, 383, 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 39.237449645996094 0.0
383 383 SER H 0.63 47.45393371582031 0.0
387 387 SER C 0.71 33.1358642578125 0.0
445 445 TYR C 0.93 54.237098693847656 0.0
450 450 SER E 1.0 36.813270568847656 0.0
1Q4O A X-ray 2.200000047683716 Monomer A 0.0 375, 383, 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 50.86332702636719 0.0
383 383 SER H 0.63 39.49446105957031 0.0
387 387 SER H 0.71 29.87346839904785 0.0
445 445 TYR C 0.93 61.55819320678711 0.0
450 450 SER E 1.0 34.91396713256836 0.0
2OJX A X-ray 2.8499999046325684 2 E 0.1 375, 383, 450
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
375 375 SER H 0.41 56.680503845214844 0.0
383 383 SER H 0.63 38.90222930908203 0.0
387 387 SER C 0.71 39.052547454833984 0.0
445 445 TYR C 0.93 45.375396728515625 0.0
450 450 SER E 1.0 41.698814392089844 0.0

Mutations

Showing 8 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
12 R L Unclassified A lung squamous cell carcinoma sample
261 L F Polymorphism
297 N D Polymorphism
332 L V Polymorphism
463 L H Polymorphism
518 R H Polymorphism
595 S L Polymorphism
599 R H Polymorphism