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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 9 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
72 SER PRIDE yes
218 SER UP, PRIDE Experimental
222 SER UP, PRIDE Experimental
231 SER PRIDE yes
286 THR UP, PRIDE Combined yes
292 THR UP, PRIDE Similarity
300 TYR PRIDE
304 SER PRIDE
386 THR PRIDE yes

3D structure is not available

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Phosphorylated amino acids are colored red on the inner ring.

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

Phospho peptides

Showing 10 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
72 71 84 2 2
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
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
218 206 227 13 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD005366 2 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture -
PXD001550 14 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 -
PXD000680 34 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
222 206 227 17 6
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 38 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD002286 26 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD005366 13 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 67 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD004452 9 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD000680 39 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
231 228 234 4 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
286 270 291 17 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 62 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 2 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
292 292 324 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 88 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
300 292 324 9 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD003531 3 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
304 292 324 13 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 53 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 -
386 363 393 24 2
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
PXD004415 3 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
386 364 393 23 2
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
PXD002286 2 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -

Structures

Showing 40 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
3EQI A X-ray 1.899999976158142 2 [CA]A:5 0.26387373 72, 218, 222, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 47.158905029296875 0.0
212 212 SER C 1.0 3.289442300796509 0.0
218 218 SER H 1.0 10.179616928100586 0.0
222 222 SER C 1.0 94.00215148925781 0.0
222 222 SER C 1.0 94.00215148925781 0.0
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 59.30607986450195 0.0
3EQH A X-ray 2.0 2 [5BM]A:1 0.20091017 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 43.53776550292969 0.0
212 212 SER C 1.0 2.0185084342956543 2.0185084342956543
218 218 SER H 1.0 22.354049682617188 0.0
222 222 SER C 1.0 88.8643569946289 0.0
231 231 SER C 1.0 0.7268297672271729 0.0
316 316 TYR H 1.0 53.58219909667969 0.0
3EQD A X-ray 2.0999999046325684 2 [CA]A:5 0.23943132 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 47.490455627441406 0.0
212 212 SER C 1.0 3.8387913703918457 0.0
218 218 SER H 1.0 12.162983894348145 0.0
222 222 SER C 1.0 94.86092376708984 0.0
231 231 SER C 1.0 0.4366033971309662 0.0
316 316 TYR H 1.0 49.956363677978516 0.0
3W8Q A X-ray 2.200000047683716 2 A 0.5650252 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 51.438873291015625 0.0
212 212 SER H 1.0 15.77795124053955 10.639398574829102
218 218 SER H 1.0 9.479402542114258 0.0
222 222 SER C 1.0 43.20281219482422 0.0
231 231 SER C 1.0 38.304237365722656 38.304237365722656
316 316 TYR H 1.0 50.92076110839844 0.0
5HZE A X-ray 2.4000000953674316 2 [MG]A:403 0.2956572 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 50.83266830444336 0.0
212 212 SER C 1.0 8.578836441040039 0.0
218 218 SER H 1.0 19.356586456298828 0.0
222 222 SER C 1.0 72.02758026123047 0.0
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 53.25494384765625 0.0
3EQG A X-ray 2.5 2 [4BM]A:1 0.16969472 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 43.59621047973633 0.0
212 212 SER C 1.0 2.620915651321411 2.2843587398529053
218 218 SER H 1.0 19.35035514831543 0.0
222 222 SER C 1.0 98.61964416503906 0.0
231 231 SER C 1.0 0.5806906223297119 0.0
316 316 TYR H 1.0 53.43657684326172 0.0
3ZLS A X-ray 2.5 Monomer [NA]A:1384 0.09977577 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 44.16597366333008 0.0
212 212 SER C 1.0 2.7445991039276123 0.0
218 218 SER C 1.0 34.74735641479492 0.0
222 222 SER C 1.0 74.99105072021484 0.0
231 231 SER C 1.0 0.2886503338813782 0.0
316 316 TYR H 1.0 53.32540512084961 0.0
3E8N A X-ray 2.5 2 A 0.34907967 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 48.95461654663086 0.0
212 212 SER C 1.0 1.809836745262146 0.0
218 218 SER H 1.0 31.251319885253906 0.0
222 222 SER C 1.0 72.43527221679688 47.53840637207031
231 231 SER C 1.0 0.14679625630378723 0.0
316 316 TYR H 1.0 45.065303802490234 0.0
4ARK A X-ray 2.5999999046325684 2 A 0.27307132 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 52.061126708984375 0.0
212 212 SER C 1.0 1.8913191556930542 0.0
218 218 SER H 1.0 35.28766632080078 0.0
222 222 SER C 1.0 59.56751251220703 13.003729820251465
231 231 SER C 1.0 0.14679625630378723 0.0
316 316 TYR H 1.0 47.330387115478516 0.0
3MBL A X-ray 2.5999999046325684 2 A 0.24399064 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 52.89863967895508 0.0
212 212 SER C 1.0 1.8683205842971802 0.0
218 218 SER H 1.0 37.441375732421875 0.0
222 222 SER C 1.0 67.5186538696289 34.20854568481445
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 46.88341522216797 0.0
3EQF A X-ray 2.700000047683716 2 [CA]A:5 0.30431277 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 43.658267974853516 0.0
212 212 SER C 1.0 3.1821627616882324 0.0
218 218 SER H 1.0 6.97644567489624 0.0
222 222 SER C 1.0 91.3362045288086 0.0
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 57.12673568725586 0.0
3PP1 A X-ray 2.700000047683716 2 A 0.38935137 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 49.9771614074707 0.0
212 212 SER C 1.0 2.113643169403076 0.0
218 218 SER H 1.0 22.593660354614258 0.0
222 222 SER C 1.0 58.09819030761719 40.37990951538086
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 46.669986724853516 0.0
4LMN A X-ray 2.799999952316284 2 A 0.34739548 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 52.93794250488281 0.0
212 212 SER C 1.0 2.8655128479003906 0.0
218 218 SER H 1.0 31.85491371154785 0.0
222 222 SER C 1.0 84.49555969238281 82.86764526367188
231 231 SER C 1.0 0.7239275574684143 0.0
316 316 TYR H 1.0 40.978553771972656 0.0
3OS3 A X-ray 2.799999952316284 2 [3OS]A:400 0.25098732 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER C 0.72 52.34683609008789 0.0
212 212 SER C 1.0 0.7258971333503723 0.7258971333503723
218 218 SER H 1.0 32.37202072143555 0.0
222 222 SER C 1.0 51.02928924560547 14.391700744628906
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 60.19532012939453 0.0
4U7Z A X-ray 2.799999952316284 2 A 0.3089829 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 46.9553337097168 0.0
212 212 SER C 1.0 1.8426934480667114 0.0
218 218 SER H 1.0 27.446603775024414 0.0
222 222 SER C 1.0 89.27398681640625 40.86681365966797
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 44.55973815917969 0.0
3ORN A X-ray 2.799999952316284 2 [SO4]A:402 0.13083391 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 48.44379425048828 0.0
212 212 SER C 1.0 1.6553529500961304 0.0
218 218 SER H 1.0 27.286569595336914 0.0
222 222 SER H 1.0 41.31559753417969 0.0
231 231 SER C 1.0 2.1869723796844482 0.0
316 316 TYR H 1.0 47.55997848510742 0.0
4MNE A X-ray 2.8499999046325684 8 B 0.53963673 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 47.57801055908203 0.0
212 212 SER C 1.0 1.897010326385498 0.0
218 218 SER H 1.0 18.654829025268555 0.0
222 222 SER C 1.0 75.63951873779297 62.330936431884766
231 231 SER C 1.0 0.5815312266349792 0.0
316 316 TYR H 1.0 41.61235809326172 0.0
5BX0 A X-ray 2.930000066757202 Monomer A 0.0 72, 218, 222, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 47.16105651855469 0.0
212 212 SER C 1.0 1.4059275388717651 0.0
218 218 SER H 1.0 25.953065872192383 0.0
222 222 SER C 1.0 51.94456100463867 0.0
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 54.351985931396484 0.0
3EQC A X-ray 1.7999999523162842 2 [3BM]A:1 0.22710298 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 46.162322998046875 0.0
212 212 SER C 1.0 3.0098154544830322 2.843871831893921
218 218 SER H 1.0 35.453330993652344 0.0
231 231 SER C 1.0 0.4363654553890228 0.0
316 316 TYR H 1.0 58.9595832824707 0.0
3VVH A X-ray 2.0 2 [4BM]A:703 0.030472485 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 43.44918441772461 0.0
212 212 SER C 1.0 2.3804116249084473 2.3804116249084473
218 218 SER H 1.0 31.577524185180664 0.0
231 231 SER C 1.0 0.29107028245925903 0.0
316 316 TYR H 1.0 53.819427490234375 0.0
3ZLY A X-ray 2.109999895095825 Monomer [NA]A:1384 0.0713727 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 45.33633804321289 0.0
212 212 SER C 1.0 2.6831092834472656 0.0
218 218 SER C 1.0 33.67183303833008 0.0
231 231 SER C 1.0 0.1443251669406891 0.0
316 316 TYR H 1.0 56.104286193847656 0.0
3ZLW A X-ray 2.119999885559082 Monomer A 0.0 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 47.5002555847168 0.0
212 212 SER C 1.0 2.4650237560272217 0.0
218 218 SER H 1.0 36.5440673828125 0.0
231 231 SER C 1.0 0.1443251669406891 0.0
316 316 TYR H 1.0 53.79021453857422 0.0
3ZLX A X-ray 2.200000047683716 Monomer [5EZ]A:1383 0.1 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 45.96921920776367 0.0
212 212 SER C 1.0 3.819169521331787 0.0
218 218 SER H 1.0 35.73399353027344 0.0
231 231 SER C 1.0 0.29046428203582764 0.0
316 316 TYR H 1.0 53.71345138549805 0.0
3DV3 A X-ray 2.299999952316284 2 A 0.2901422 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 49.266754150390625 0.0
212 212 SER C 1.0 2.0125598907470703 0.0
218 218 SER H 1.0 21.00932502746582 0.0
231 231 SER C 1.0 0.14377711713314056 0.0
316 316 TYR H 1.0 47.29191970825195 0.0
3ZM4 A X-ray 2.369999885559082 Monomer [22T]A:1383 0.1 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 49.2038459777832 0.0
212 212 SER C 1.0 2.494248390197754 0.0
218 218 SER H 1.0 33.89247131347656 0.0
231 231 SER C 1.0 0.2902263402938843 0.0
316 316 TYR H 1.0 52.26298522949219 0.0
1S9J A X-ray 2.4000000953674316 2 A 0.38086325 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 55.24324035644531 0.0
212 212 SER C 1.0 2.5486600399017334 0.0
218 218 SER H 1.0 32.175533294677734 0.0
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 52.10396194458008 0.0
3EQB A X-ray 2.619999885559082 2 A 0.42166376 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 55.61248779296875 0.0
212 212 SER C 1.0 2.447652578353882 0.0
218 218 SER C 1.0 38.52118682861328 0.0
231 231 SER C 1.0 0.43736961483955383 0.0
316 316 TYR H 1.0 47.62281036376953 0.0
5EYM A X-ray 2.700000047683716 2 [5U5]A:401 0.2961371 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 45.5411262512207 0.0
212 212 SER C 1.0 4.200027942657471 0.0
218 218 SER H 1.0 41.4213981628418 0.0
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 61.070228576660156 0.0
3V01 A X-ray 2.700000047683716 2 A 0.33093998 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 55.02281188964844 0.0
212 212 SER C 1.0 2.1553235054016113 0.0
218 218 SER H 1.0 26.660993576049805 0.0
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 45.897727966308594 0.0
4U81 A X-ray 2.700000047683716 2 A 0.38137597 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 51.49765396118164 0.0
212 212 SER C 1.0 2.8645105361938477 0.0
218 218 SER H 1.0 31.79625129699707 0.0
231 231 SER C 1.0 0.14679625630378723 0.0
316 316 TYR H 1.0 43.855735778808594 0.0
3DY7 A X-ray 2.700000047683716 2 A 0.3366023 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 49.9896125793457 0.0
212 212 SER C 1.0 3.34384822845459 0.0
218 218 SER H 1.0 27.850526809692383 0.0
231 231 SER C 1.0 0.2905733585357666 0.0
316 316 TYR H 1.0 47.233890533447266 0.0
3V04 A X-ray 2.700000047683716 2 A 0.3376046 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 53.52655029296875 0.0
212 212 SER C 1.0 2.645364284515381 0.0
218 218 SER H 1.0 26.28142547607422 0.0
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 45.78710174560547 0.0
2P55 A X-ray 2.799999952316284 2 A 0.41643035 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 56.348026275634766 0.0
212 212 SER C 1.0 2.969985246658325 0.0
218 218 SER H 1.0 29.428634643554688 0.0
231 231 SER C 1.0 0.0 0.0
316 316 TYR H 1.0 54.10637664794922 0.0
4U80 A X-ray 2.799999952316284 2 A 0.36980549 72, 218, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 55.825653076171875 0.0
212 212 SER C 1.0 3.0060787200927734 0.0
218 218 SER H 1.0 35.15345764160156 0.0
231 231 SER C 1.0 0.14679625630378723 0.0
316 316 TYR H 1.0 41.8577766418457 0.0
4AN3 A X-ray 2.0999999046325684 Monomer [ATP]A:1383 0.02681131 72, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 54.878360748291016 0.0
212 212 SER C 1.0 2.0974655151367188 0.0
231 231 SER C 1.0 0.2921797037124634 0.0
316 316 TYR H 1.0 67.02584838867188 0.0
4ANB A X-ray 2.200000047683716 Monomer [ACP]A:1383 0.03273428 72, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 48.37671661376953 0.0
212 212 SER C 1.0 2.0108306407928467 0.0
231 231 SER C 1.0 0.43888404965400696 0.0
316 316 TYR H 1.0 63.66183090209961 0.0
3SLS A X-ray 2.299999952316284 Monomer [77D]A:500 0.043431368 72, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 54.5323600769043 0.0
212 212 SER C 1.0 31.02444076538086 15.533477783203125
231 231 SER C 1.0 0.0 0.0
316 278 TYR H 1.0 80.92707824707031 0.0
4AN2 A X-ray 2.5 Monomer [ACP]A:1383 0.025978096 72, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 45.84292984008789 0.0
212 212 SER C 1.0 1.6184208393096924 0.0
231 231 SER C 1.0 0.5855883955955505 0.0
316 316 TYR H 1.0 58.854984283447266 0.0
4AN9 A X-ray 2.799999952316284 Monomer [ACP]A:1382 0.024479387 72, 231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 72 SER E 0.72 53.48583221435547 0.0
212 212 SER C 1.0 1.109702229499817 0.0
231 231 SER C 1.0 0.43888404965400696 0.0
316 316 TYR H 1.0 68.70700073242188 0.0
3WIG A X-ray 2.700000047683716 2 [CL]A:405 0.11618092
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
72 73 SER E 0.72 53.57724380493164 0.0
212 213 SER C 1.0 1.4347190856933594 0.0
218 219 SER H 1.0 31.558916091918945 0.0
222 223 SER H 1.0 46.64071273803711 0.0
231 232 SER C 1.0 2.332504987716675 0.0
316 316 TYR H 1.0 50.691707611083984 0.0

Mutations

Showing 3 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
53 F S Disease Cardiofaciocutaneous syndrome 3 (CFC3) [MIM:615279]
128 G V Disease Cardiofaciocutaneous syndrome 3 (CFC3) [MIM:615279]
130 Y C Disease Cardiofaciocutaneous syndrome 3 (CFC3) [MIM:615279]