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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
21 THR PRIDE yes
24 THR UP, PRIDE Combined yes
32 THR PRIDE yes
135 SER PRIDE yes
146 TYR PRIDE yes
147 TYR PRIDE yes
155 TYR 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 9 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
21 13 23 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
24 13 28 12 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
32 29 37 4 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
135 133 140 3 5
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
PXD003531 5 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD006482 5 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
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 -
135 135 140 1 9
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 9 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000836 12 HOPE-fixation of lung tissue allows retrospective proteome and phosphoproteome studies Homo sapiens (Human) PARTIAL 2014-05-22 lung -
PXD000612 17 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD002436 2 Monitoring cellular phosphorylation signaling pathways into chromatin and down to the gene level Homo sapiens (Human) COMPLETE 2015-11-09 HeLa cell -
PXD004940 1 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD003531 39 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD005366 5 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 -
PXD000680 10 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
135 135 141 1 2
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
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
146 143 152 4 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 4 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001565 2 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
PXD003198 2 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
147 143 152 5 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 29 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001565 5 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003198 15 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line
155 153 166 3 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001565 5 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain

Structures

Showing 62 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
3GJ0 A X-ray 1.4800000190734863 2 [GDP]A:302 0.3907465 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 56.3823356628418 22.480777740478516
32 32 THR H 1.0 64.230712890625 0.0
135 135 SER H 1.0 59.52861404418945 0.0
146 146 TYR E 1.0 12.927322387695312 0.0
147 147 TYR E 1.0 41.13058853149414 0.0
155 155 TYR E 1.0 26.881908416748047 0.0
5CIQ A X-ray 1.649999976158142 2 [GDP]A:301 0.417401 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.1443251669406891 0.1443251669406891
24 24 THR H 0.68 57.005008697509766 23.230710983276367
32 32 THR H 1.0 72.2435531616211 0.0
135 135 SER H 1.0 48.167564392089844 0.0
146 146 TYR E 1.0 12.83338737487793 0.0
147 147 TYR E 1.0 40.83797836303711 0.0
155 155 TYR E 1.0 28.406726837158203 0.0
5CIW A X-ray 1.75 2 [GDP]A:301 0.39774325 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 58.55044937133789 23.287933349609375
32 32 THR H 1.0 70.83785247802734 0.0
135 135 SER H 1.0 62.05610275268555 0.0
146 146 TYR E 1.0 11.541695594787598 0.0
147 147 TYR E 1.0 42.02587890625 0.0
155 155 TYR E 1.0 28.948139190673828 0.0
5CJ2 A X-ray 1.75 4 [GDP]A:301 0.42011032 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.145799919962883 0.145799919962883
24 24 THR H 0.68 60.59822082519531 22.810527801513672
32 32 THR H 1.0 73.24201965332031 0.0
135 135 SER H 1.0 49.35134506225586 0.0
146 146 TYR E 1.0 12.155920028686523 0.0
147 147 TYR E 1.0 41.98118209838867 0.0
155 155 TYR E 1.0 30.114482879638672 0.0
5CIT A X-ray 1.75 2 [GDP]A:301 0.3986828 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.16729053854942322 0.0
24 24 THR H 0.68 60.77263641357422 23.906879425048828
32 32 THR H 1.0 69.95476531982422 0.0
135 135 SER H 1.0 51.961612701416016 0.0
146 146 TYR E 1.0 10.648416519165039 0.0
147 147 TYR E 1.0 38.676753997802734 0.0
155 155 TYR E 1.0 28.443506240844727 0.0
4HAT A X-ray 1.7799999713897705 3 B 0.59744567 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.16348005831241608 0.0
24 24 THR H 0.68 32.761898040771484 0.0
32 32 THR H 1.0 94.66680908203125 51.73794937133789
135 135 SER H 1.0 48.48710250854492 0.0
146 146 TYR E 1.0 38.4423713684082 0.0
147 147 TYR E 1.0 42.64260482788086 0.0
155 155 TYR C 1.0 123.80903625488281 0.0
3GJ5 A X-ray 1.7899999618530273 Monomer [GDP]A:302 0.043156136 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 55.933467864990234 21.831951141357422
32 32 THR H 1.0 58.73368835449219 0.0
135 135 SER H 1.0 60.321678161621094 0.0
146 146 TYR E 1.0 12.21479320526123 0.0
147 147 TYR E 1.0 40.30498123168945 0.0
155 155 TYR E 1.0 27.330991744995117 0.0
3GJ3 A X-ray 1.7899999618530273 2 [GDP]A:302 0.3682666 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 56.340763092041016 21.631132125854492
32 32 THR H 1.0 64.2386474609375 0.0
135 135 SER H 1.0 54.6749153137207 0.0
146 146 TYR E 1.0 11.422842025756836 0.0
147 147 TYR E 1.0 40.15639877319336 0.0
155 155 TYR E 1.0 26.80803680419922 0.0
4WVF A X-ray 1.7999999523162842 3 B 0.6070932 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 34.02195358276367 0.0
32 32 THR H 1.0 94.12836456298828 52.8263053894043
135 135 SER H 1.0 47.39981460571289 0.0
146 146 TYR E 1.0 38.0663948059082 0.0
147 147 TYR E 1.0 42.14068603515625 0.0
155 155 TYR C 1.0 123.0594253540039 0.0
4HB2 A X-ray 1.7999999523162842 3 B 0.51399165 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.30784597992897034 0.0
24 24 THR H 0.68 31.887338638305664 0.0
32 32 THR H 1.0 95.42240142822266 56.470436096191406
135 135 SER H 1.0 62.50146484375 0.0
146 146 TYR E 1.0 38.00320053100586 0.0
147 147 TYR E 1.0 39.627220153808594 0.0
155 155 TYR C 1.0 117.60370635986328 0.0
3GJ8 A X-ray 1.8200000524520874 2 [GDP]A:302 0.27747267 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 55.127471923828125 22.304128646850586
32 32 THR H 1.0 62.61029052734375 0.0
135 135 SER H 1.0 57.28091049194336 0.0
146 146 TYR E 1.0 11.761573791503906 0.0
147 147 TYR E 1.0 39.55460739135742 0.0
155 155 TYR E 1.0 28.32830238342285 0.0
4HAZ A X-ray 1.899999976158142 3 B 0.50543773 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 32.021385192871094 0.0
32 32 THR H 1.0 95.32171630859375 52.512229919433594
135 135 SER H 1.0 48.48549270629883 0.0
146 146 TYR E 1.0 36.38615798950195 0.0
147 147 TYR E 1.0 41.56990432739258 0.0
155 155 TYR C 1.0 123.43545532226562 0.0
4HAW A X-ray 1.899999976158142 3 B 0.585772 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.16348005831241608 0.0
24 24 THR H 0.68 35.71281051635742 0.0
32 32 THR H 1.0 94.994873046875 57.028907775878906
135 135 SER H 1.0 48.02431106567383 0.0
146 146 TYR E 1.0 39.257896423339844 0.0
147 147 TYR E 1.0 40.28464889526367 0.0
155 155 TYR C 1.0 122.24276733398438 0.0
3GJ7 A X-ray 1.9299999475479126 2 [GDP]A:302 0.24156675 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 58.27909469604492 23.478464126586914
32 32 THR H 1.0 56.53742218017578 0.0
135 135 SER H 1.0 55.9580192565918 0.0
146 146 TYR E 1.0 10.971939086914062 0.0
147 147 TYR E 1.0 40.342899322509766 0.0
155 155 TYR E 1.0 27.675617218017578 0.0
4HAV A X-ray 2.0 3 B 0.51971346 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.16348005831241608 0.0
24 24 THR H 0.68 31.96286392211914 0.0
32 32 THR H 1.0 96.26187896728516 60.73979568481445
135 135 SER H 1.0 47.5934944152832 0.0
146 146 TYR E 1.0 37.9305534362793 0.0
147 147 TYR E 1.0 40.4234504699707 0.0
155 155 TYR C 1.0 118.03494262695312 0.0
4HAU A X-ray 2.0 3 B 0.57194763 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.16348005831241608 0.0
24 24 THR H 0.68 40.09797668457031 0.0
32 32 THR H 1.0 96.54884338378906 53.98586654663086
135 135 SER H 1.0 47.08402633666992 0.0
146 146 TYR E 1.0 37.95991134643555 0.0
147 147 TYR E 1.0 42.066959381103516 0.0
155 155 TYR C 1.0 123.03485107421875 0.0
4HB4 A X-ray 2.049999952316284 3 B 0.608453 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 31.80287742614746 0.0
32 32 THR H 1.0 92.85928344726562 51.92852020263672
135 135 SER H 1.0 49.46572494506836 0.0
146 146 TYR E 1.0 37.56212615966797 0.0
147 147 TYR E 1.0 41.0628547668457 0.0
155 155 TYR C 1.0 120.5719985961914 0.0
5UWP A X-ray 2.049999952316284 2 B 0.64812624 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.16348005831241608 0.0
24 24 THR H 0.68 35.35747146606445 0.0
32 32 THR H 1.0 93.13301086425781 42.68153762817383
135 135 SER H 1.0 59.95260238647461 0.0
146 146 TYR E 1.0 37.9068603515625 0.0
147 147 TYR E 1.0 37.947078704833984 0.0
155 155 TYR C 1.0 116.1373519897461 0.0
5DIF A X-ray 2.0899999141693115 8 B 0.63721275 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.16348005831241608 0.0
24 24 THR H 0.68 35.919708251953125 0.0
32 32 THR H 1.0 94.40450286865234 57.28324508666992
135 135 SER H 1.0 58.88315963745117 0.0
146 146 TYR E 1.0 39.25259017944336 0.0
147 147 TYR E 1.0 37.89892578125 0.0
155 155 TYR C 1.0 115.19590759277344 0.0
3CH5 A X-ray 2.0999999046325684 8 [GDP]A:220 0.2702411 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.14377711713314056 0.14377711713314056
24 24 THR H 0.68 61.527103424072266 22.386690139770508
32 32 THR H 1.0 66.44322967529297 0.0
135 135 SER H 1.0 57.26826095581055 0.0
146 146 TYR E 1.0 22.85677719116211 0.0
147 147 TYR E 1.0 38.17779541015625 0.0
155 155 TYR E 1.0 36.13664245605469 0.0
4GMX A X-ray 2.0999999046325684 3 B 0.5942925 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.16348005831241608 0.0
24 24 THR H 0.68 33.04831314086914 0.0
32 32 THR H 1.0 93.38249969482422 57.21363067626953
135 135 SER H 1.0 54.24947738647461 0.0
146 146 TYR E 1.0 38.579437255859375 0.0
147 147 TYR E 1.0 39.151371002197266 0.0
155 155 TYR C 1.0 121.09526824951172 0.0
5UWI A X-ray 2.140000104904175 4 B 0.63010037 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 40.09951400756836 0.0
32 32 THR H 1.0 94.99100494384766 54.85481262207031
135 135 SER H 1.0 65.00086212158203 0.0
146 146 TYR E 1.0 37.05405807495117 0.0
147 147 TYR E 1.0 39.22376251220703 0.0
155 155 TYR C 1.0 115.68193817138672 0.0
5UWW A X-ray 2.1500000953674316 4 B 0.6094735 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.1460898518562317 0.0
24 24 THR H 0.68 36.9686393737793 0.0
32 32 THR H 1.0 93.30328369140625 54.99321746826172
135 135 SER H 1.0 58.419429779052734 0.0
146 146 TYR E 1.0 39.2244987487793 0.0
147 147 TYR E 1.0 39.38136672973633 0.0
155 155 TYR C 1.0 118.5624771118164 0.0
3GJ4 A X-ray 2.1500000953674316 Monomer [GDP]A:302 0.044087823 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 56.49492263793945 23.022539138793945
32 32 THR H 1.0 62.493385314941406 0.0
135 135 SER H 1.0 63.58102035522461 0.0
146 146 TYR E 1.0 9.917533874511719 0.0
147 147 TYR E 1.0 39.731937408447266 0.0
155 155 TYR E 1.0 30.22319984436035 0.0
4HB0 A X-ray 2.200000047683716 3 B 0.60047454 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 30.26177978515625 0.0
32 32 THR H 1.0 94.77120208740234 51.58921813964844
135 135 SER H 1.0 46.64863967895508 0.0
146 146 TYR E 1.0 38.48994064331055 0.0
147 147 TYR E 1.0 40.70256423950195 0.0
155 155 TYR C 1.0 121.27498626708984 0.0
5UWJ A X-ray 2.2200000286102295 2 B 0.62926275 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.3095698952674866 0.0
24 24 THR H 0.68 39.36794662475586 0.0
32 32 THR H 1.0 94.03034210205078 45.15415954589844
135 135 SER H 1.0 54.09356689453125 0.0
146 146 TYR E 1.0 38.70880126953125 0.0
147 147 TYR E 1.0 37.38052749633789 0.0
155 155 TYR C 1.0 114.54757690429688 0.0
4GPT A X-ray 2.2200000286102295 3 B 0.5591438 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 35.62431335449219 0.0
32 32 THR H 1.0 94.02863311767578 57.7864990234375
135 135 SER H 1.0 54.21235275268555 0.0
146 146 TYR E 1.0 38.49900817871094 0.0
147 147 TYR E 1.0 40.418766021728516 0.0
155 155 TYR C 1.0 123.16236114501953 0.0
5UWR A X-ray 2.240000009536743 4 B 0.6193138 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.3095698952674866 0.0
24 24 THR H 0.68 37.7351188659668 0.0
32 32 THR H 1.0 95.74555206298828 55.73955535888672
135 135 SER H 1.0 62.25749969482422 0.0
146 146 TYR E 1.0 36.65690612792969 0.0
147 147 TYR E 1.0 37.99277114868164 0.0
155 155 TYR C 1.0 114.86282348632812 0.0
5UWU A X-ray 2.240000009536743 4 B 0.6482013 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.1460898518562317 0.0
24 24 THR H 0.68 37.976070404052734 0.0
32 32 THR H 1.0 95.2972640991211 47.963539123535156
135 135 SER H 1.0 56.70359420776367 0.0
146 146 TYR E 1.0 40.54819869995117 0.0
147 147 TYR E 1.0 38.77367401123047 0.0
155 155 TYR C 1.0 116.06847381591797 0.0
5UWH A X-ray 2.259999990463257 4 B 0.61827075 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.3095698952674866 0.0
24 24 THR H 0.68 36.82118606567383 0.0
32 32 THR H 1.0 95.28154754638672 56.37281799316406
135 135 SER H 1.0 63.48204803466797 0.0
146 146 TYR E 1.0 38.149757385253906 0.0
147 147 TYR E 1.0 37.22366714477539 0.0
155 155 TYR C 1.0 115.07302856445312 0.0
5DI9 A X-ray 2.2799999713897705 4 B 0.60606086 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.3095698952674866 0.0
24 24 THR H 0.68 37.888954162597656 0.0
32 32 THR H 1.0 97.23723602294922 46.42728805541992
135 135 SER H 1.0 63.39638900756836 0.0
146 146 TYR E 1.0 39.47633361816406 0.0
147 147 TYR E 1.0 37.359527587890625 0.0
155 155 TYR C 1.0 115.63265228271484 0.0
4HAX A X-ray 2.2799999713897705 3 B 0.6087981 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 33.2845344543457 0.0
32 32 THR H 1.0 97.37076568603516 60.45293045043945
135 135 SER H 1.0 50.68694305419922 0.0
146 146 TYR E 1.0 38.63047409057617 0.0
147 147 TYR E 1.0 40.164249420166016 0.0
155 155 TYR C 1.0 119.83000183105469 0.0
5UWQ A X-ray 2.2799999713897705 4 B 0.6013671 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.1460898518562317 0.0
24 24 THR H 0.68 38.98421096801758 0.0
32 32 THR H 1.0 94.73370361328125 42.97489929199219
135 135 SER H 1.0 64.1618881225586 0.0
146 146 TYR E 1.0 38.9371452331543 0.0
147 147 TYR E 1.0 39.40171432495117 0.0
155 155 TYR C 1.0 115.66181182861328 0.0
5DHF A X-ray 2.2899999618530273 4 B 0.6079897 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.1460898518562317 0.0
24 24 THR H 0.68 37.9610710144043 0.0
32 32 THR H 1.0 96.53507995605469 50.59992599487305
135 135 SER H 1.0 48.25830841064453 0.0
146 146 TYR E 1.0 40.11936569213867 0.0
147 147 TYR E 1.0 38.88394546508789 0.0
155 155 TYR C 1.0 116.46607971191406 0.0
1IBR A X-ray 2.299999952316284 2 B 0.40952832 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 38.82103729248047 0.0
32 32 THR H 1.0 89.91773223876953 0.0
135 135 SER H 1.0 61.018402099609375 0.0
146 146 TYR E 1.0 37.21715545654297 4.989596843719482
147 147 TYR E 1.0 33.080535888671875 22.32378387451172
155 155 TYR C 1.0 110.47655487060547 0.0
4HAY A X-ray 2.299999952316284 3 B 0.60106474 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 34.510990142822266 0.0
32 32 THR H 1.0 97.13324737548828 53.44867706298828
135 135 SER H 1.0 49.32239532470703 0.0
146 146 TYR E 1.0 40.03950119018555 0.0
147 147 TYR E 1.0 39.72284698486328 0.0
155 155 TYR C 1.0 123.63003540039062 0.0
5UWT A X-ray 2.3399999141693115 4 B 0.6415483 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 36.34380340576172 0.0
32 32 THR H 1.0 94.72430419921875 43.07118606567383
135 135 SER H 1.0 63.97344207763672 0.0
146 146 TYR E 1.0 38.1506462097168 0.0
147 147 TYR E 1.0 39.659393310546875 0.0
155 155 TYR C 1.0 118.60641479492188 0.0
5UWO A X-ray 2.3499999046325684 2 B 0.62157625 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.1460898518562317 0.0
24 24 THR H 0.68 38.4276123046875 0.0
32 32 THR H 1.0 92.46692657470703 41.666114807128906
135 135 SER H 1.0 65.57110595703125 0.0
146 146 TYR E 1.0 38.20609664916992 0.0
147 147 TYR E 1.0 38.114315032958984 0.0
155 155 TYR C 1.0 116.38261413574219 0.0
5UWS A X-ray 2.4000000953674316 4 B 0.59406483 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.1460898518562317 0.0
24 24 THR H 0.68 35.324012756347656 0.0
32 32 THR H 1.0 101.38822174072266 37.876956939697266
135 135 SER H 1.0 63.89122772216797 0.0
146 146 TYR E 1.0 38.15084457397461 0.0
147 147 TYR E 1.0 37.71847152709961 0.0
155 155 TYR C 1.0 117.70600891113281 0.0
5CLL A X-ray 2.450000047683716 2 B 0.4688932 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.14679625630378723 0.0
24 24 THR H 0.68 33.5118408203125 0.0
32 32 THR H 1.0 95.5095443725586 60.290523529052734
135 135 SER H 1.0 57.33563995361328 0.0
146 146 TYR E 1.0 35.273502349853516 0.0
147 147 TYR E 1.0 35.60669708251953 0.0
155 155 TYR C 1.0 116.52098083496094 1.3456904888153076
3GJX C X-ray 2.5 3 A 0.4639139 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.2928873896598816 0.0
24 24 THR H 0.68 33.40877151489258 0.0
32 32 THR C 1.0 69.37451934814453 0.0
135 135 SER H 1.0 43.026885986328125 0.0
146 146 TYR E 1.0 41.969669342041016 36.94394302368164
147 147 TYR E 1.0 43.61078643798828 0.0
155 155 TYR C 1.0 108.48129272460938 98.03367614746094
5JLJ A X-ray 2.5 3 B 0.49799705 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.14436592161655426 0.0
24 24 THR H 0.68 36.51472473144531 0.0
32 32 THR H 1.0 92.26793670654297 56.4114875793457
135 135 SER H 1.0 61.66372299194336 0.0
146 146 TYR E 1.0 37.843299865722656 0.0
147 147 TYR E 1.0 40.523406982421875 0.0
155 155 TYR C 1.0 121.41177368164062 0.0
3EA5 A X-ray 2.5 Monomer [GDP]A:220 0.040587645 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 31.0760555267334 18.18330955505371
32 32 THR H 1.0 87.5811538696289 0.0
135 135 SER C 1.0 70.17828369140625 0.0
146 146 TYR E 1.0 19.72653579711914 0.0
147 147 TYR E 1.0 32.86014175415039 0.0
155 155 TYR C 1.0 118.5499496459961 0.0
5DH9 A X-ray 2.549999952316284 8 B 0.58117324 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.3095698952674866 0.0
24 24 THR H 0.68 39.18159866333008 0.0
32 32 THR C 1.0 99.52509307861328 41.90712356567383
135 135 SER H 1.0 61.69641876220703 0.0
146 146 TYR E 1.0 39.70198059082031 0.0
147 147 TYR E 1.0 38.48994445800781 0.0
155 155 TYR C 1.0 116.48416137695312 0.0
3GJ6 A X-ray 2.700000047683716 2 [GDP]A:302 0.039377067 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 57.23869705200195 22.346405029296875
32 32 THR H 1.0 65.8546142578125 0.0
135 135 SER H 1.0 57.08998489379883 0.0
146 146 TYR E 1.0 10.241130828857422 0.0
147 147 TYR E 1.0 35.01498031616211 0.0
155 155 TYR E 1.0 32.43730163574219 0.0
1K5D A X-ray 2.700000047683716 3 B 0.6384251 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 1.4873393774032593 0.0
24 24 THR H 0.68 39.48149490356445 0.0
32 32 THR H 1.0 82.78662872314453 49.39154815673828
135 135 SER C 1.0 63.36476135253906 0.0
146 146 TYR E 1.0 28.92620277404785 0.0
147 147 TYR E 1.0 42.75132369995117 0.0
155 155 TYR C 1.0 119.16622924804688 0.0
3NBZ C X-ray 2.799999952316284 3 A 0.41334888 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.5839447379112244 0.0
24 24 THR H 0.68 50.746742248535156 0.0
32 32 THR C 1.0 77.30301666259766 0.0
135 135 SER C 1.0 47.06240463256836 0.0
146 146 TYR E 1.0 38.4586296081543 31.951154708862305
147 147 TYR E 1.0 40.812232971191406 0.8714348673820496
155 155 TYR C 1.0 104.88404083251953 96.62749481201172
4HB3 A X-ray 2.799999952316284 3 B 0.5801816 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.14436592161655426 0.0
24 24 THR H 0.68 39.40216064453125 0.0
32 32 THR C 1.0 97.24632263183594 55.01052474975586
135 135 SER C 1.0 48.52203369140625 0.0
146 146 TYR E 1.0 36.20537567138672 0.0
147 147 TYR E 1.0 37.88063049316406 0.0
155 155 TYR E 1.0 121.86979675292969 0.0
5DIS B X-ray 2.8499999046325684 4 A 0.26910406 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.8749268054962158 0.0
24 24 THR H 0.68 32.6707878112793 0.0
32 32 THR C 1.0 100.30229187011719 0.0
135 135 SER H 1.0 55.559906005859375 0.0
146 146 TYR E 1.0 39.15176010131836 32.83499526977539
147 147 TYR E 1.0 34.66358184814453 0.0
155 155 TYR C 1.0 110.23609161376953 100.85202026367188
4OL0 A X-ray 2.9000000953674316 2 [GTP]A:302 0.37527594 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.3132460415363312 0.14553771913051605
24 24 THR H 0.68 32.74053192138672 18.16354751586914
32 32 THR C 1.0 145.13275146484375 0.0
135 135 SER H 1.0 41.68165969848633 0.0
146 146 TYR E 1.0 21.108440399169922 0.0
147 147 TYR E 1.0 40.42168045043945 0.0
155 155 TYR E 1.0 111.65531158447266 0.0
3NC0 C X-ray 2.9000000953674316 3 A 0.7396556 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.7262470722198486 0.0
24 24 THR H 0.68 37.27444076538086 0.0
32 32 THR H 1.0 83.6903076171875 0.0
135 135 SER H 1.0 41.81618881225586 0.0
146 146 TYR E 1.0 37.21255874633789 31.385786056518555
147 147 TYR E 1.0 48.255714416503906 0.0
155 155 TYR E 1.0 105.96735382080078 97.72501373291016
5DHA A X-ray 2.950000047683716 2 B 0.5987981 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.1460898518562317 0.0
24 24 THR H 0.68 35.79158401489258 0.0
32 32 THR C 1.0 95.46269989013672 44.859893798828125
135 135 SER C 1.0 53.94734191894531 0.0
146 146 TYR E 1.0 38.90779113769531 0.0
147 147 TYR E 1.0 41.070030212402344 0.0
155 155 TYR E 1.0 115.49263000488281 0.0
1RRP A X-ray 2.9600000381469727 8 B 0.595316 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.33323413133621216 0.0
24 24 THR H 0.68 34.72855758666992 0.0
32 32 THR H 1.0 88.75595092773438 69.6724624633789
135 135 SER H 1.0 54.64458465576172 0.0
146 146 TYR E 1.0 33.25552749633789 0.0
147 147 TYR E 1.0 37.79585647583008 0.0
155 155 TYR E 1.0 108.88724517822266 3.1851413249969482
1QBK C X-ray 3.0 4 B 0.38026378 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 2.8377952575683594 0.0
24 24 THR H 0.68 45.62112808227539 0.0
32 32 THR C 1.0 49.09355926513672 0.0
135 135 SER H 1.0 59.17501449584961 0.0
146 146 TYR E 1.0 35.480838775634766 35.32396697998047
147 147 TYR E 1.0 44.8088264465332 10.114242553710938
155 155 TYR E 1.0 115.80696105957031 94.12496948242188
1K5G A X-ray 3.0999999046325684 3 B 0.59818244 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 2.1006722450256348 0.0
24 24 THR H 0.68 35.116397857666016 0.0
32 32 THR H 1.0 88.68849182128906 59.65892791748047
135 135 SER C 1.0 74.96353912353516 0.0
146 146 TYR E 1.0 29.06247901916504 0.0
147 147 TYR E 1.0 43.24872589111328 0.0
155 155 TYR C 1.0 125.25267028808594 0.0
5CLQ A X-ray 3.200000047683716 4 B 0.3745953 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 30.58101463317871 0.0
32 32 THR H 1.0 92.11415100097656 58.93880081176758
135 135 SER H 1.0 60.17607498168945 0.0
146 146 TYR E 1.0 21.93196678161621 0.0
147 147 TYR E 1.0 40.97100067138672 0.0
155 155 TYR C 1.0 115.41802215576172 0.5011906623840332
5DLQ C X-ray 3.200000047683716 3 B 0.41669613 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.0 0.0
24 24 THR H 0.68 33.542381286621094 0.0
32 32 THR C 1.0 102.53453063964844 0.0
135 135 SER H 1.0 60.12366485595703 0.0
146 146 TYR E 1.0 29.02667808532715 0.0
147 147 TYR E 1.0 42.386356353759766 9.812758445739746
155 155 TYR E 1.0 104.52021026611328 82.73468780517578
3NC1 C X-ray 3.3499999046325684 2 A 0.4894977 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 1.1707593202590942 0.0
24 24 THR H 0.68 31.022567749023438 0.0
32 32 THR C 1.0 89.83856201171875 0.0
135 135 SER H 1.0 69.35484313964844 0.0
146 146 TYR E 1.0 42.92509460449219 35.07191848754883
147 147 TYR E 1.0 31.691362380981445 0.0
155 155 TYR C 1.0 124.45787048339844 116.21672821044922
4C0Q C X-ray 3.4200000762939453 Monomer [GTP]C:1179 0.05670827 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.16589675843715668 0.0
24 24 THR H 0.68 39.51639938354492 17.57587432861328
32 32 THR C 1.0 80.72244262695312 0.0
135 135 SER H 1.0 68.89427947998047 0.0
146 146 TYR E 1.0 22.809839248657227 0.0
147 147 TYR E 1.0 37.685691833496094 0.0
155 155 TYR C 1.0 111.98150634765625 0.0
3NBY C X-ray 3.4200000762939453 6 A 0.469721 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 1.3538553714752197 0.0
24 24 THR H 0.68 35.505584716796875 0.0
32 32 THR C 1.0 72.23040008544922 0.0
135 135 SER H 1.0 39.835391998291016 0.0
146 146 TYR E 1.0 38.30104064941406 32.44860076904297
147 147 TYR E 1.0 49.67552185058594 0.0
155 155 TYR C 1.0 101.08846282958984 96.1220703125
3ZJY A X-ray 3.5999999046325684 4 B 0.40770823 21, 24, 32, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 10.576878547668457 0.0
24 24 THR H 0.68 55.71158218383789 0.0
32 32 THR C 1.0 97.88577270507812 0.0
135 135 SER C 1.0 54.898521423339844 0.0
146 146 TYR E 1.0 53.878257751464844 0.0
147 147 TYR E 1.0 52.21649932861328 5.0328240394592285
155 155 TYR E 1.0 115.29638671875 0.0
1I2M A X-ray 1.7599999904632568 4 [SO4]A:1250 0.537881 21, 24, 135, 146, 147, 155
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
21 21 THR C 0.5 0.29045578837394714 0.29045578837394714
24 24 THR H 0.68 76.5147705078125 16.146514892578125
135 135 SER C 1.0 1.8432782888412476 0.0
146 146 TYR E 1.0 22.401195526123047 0.0
147 147 TYR E 1.0 38.96506881713867 0.0
155 155 TYR E 1.0 117.31902313232422 0.0

Mutations

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