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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 12 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
2 SER UP Combined
4 SER UP Combined
57 SER PRIDE yes
62 SER PRIDE yes
76 TYR UP, PRIDE Similarity yes
115 SER PRIDE yes
161 TYR PRIDE yes
175 SER PRIDE yes
196 TYR UP, PRIDE Combined yes
203 SER UP, PRIDE Combined yes
271 SER PRIDE yes
399 SER 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 12 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
57 57 75 1 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
62 57 75 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
76 57 86 20 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
76 67 86 10 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
76 76 86 1 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 9 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 -
115 107 123 9 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
161 157 171 5 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 -
PXD001565 1 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
175 172 184 4 3
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
PXD006482 1 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 -
196 193 199 4 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 30 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
PXD003198 10 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
203 200 216 4 16
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 10 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD001060 203 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000474 10 Simulated phosphopeptide spectral library for confident site localization Homo sapiens (Human) PARTIAL 2015-03-17 HeLa cell -
PXD003531 61 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD004940 3 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD001333 6 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD006482 5 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 49 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 58 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD002394 2 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture -
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 -
PXD004452 73 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 -
PXD000612 52 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 88 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
PXD001546 24 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
271 268 279 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD005366 1 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture
399 389 406 11 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

Structures

Showing 24 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
2X13 A X-ray 1.7400000095367432 Monomer [3PG]A:1419 0.033580404 4, 57, 62, 76, 115, 161, 175, 196, 203, 271, 399
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 4 SER C 1.0 120.1550064086914 0.0
57 57 SER E 0.86 0.0 0.0
62 62 SER C 1.0 0.0 0.0
76 76 TYR H 0.93 62.44170379638672 0.0
115 115 SER E 0.78 27.785268783569336 0.0
161 161 TYR E 1.0 6.248653411865234 0.0
175 175 SER H 1.0 0.0 0.0
196 196 TYR H 1.0 56.44138717651367 0.0
203 203 SER C 0.37 87.532958984375 0.0
271 271 SER H 0.78 68.48957061767578 0.0
399 399 SER H 1.0 3.123544931411743 0.0
4AXX A X-ray 1.7400000095367432 Monomer [ADP]A:1420 0.025699968 4, 57, 62, 76, 115, 161, 175, 196, 203, 271, 399
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 4 SER C 1.0 112.96681213378906 0.0
57 57 SER E 0.86 0.0 0.0
62 62 SER C 1.0 0.0 0.0
76 76 TYR H 0.93 67.6150894165039 0.0
115 115 SER E 0.78 27.917190551757812 0.0
161 161 TYR E 1.0 5.778104782104492 0.0
175 175 SER H 1.0 0.0 0.0
196 196 TYR H 1.0 57.31991958618164 0.0
203 203 SER C 0.37 89.52196502685547 0.0
271 271 SER H 0.78 72.43402099609375 0.0
399 399 SER H 1.0 2.5412542819976807 0.0
2X14 A X-ray 1.899999976158142 Monomer [3PG]A:1419 0.036058523 4, 57, 62, 76, 115, 161, 175, 196, 203, 271, 399
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 4 SER C 1.0 118.34410095214844 0.0
57 57 SER E 0.86 0.0 0.0
62 62 SER C 1.0 0.0 0.0
76 76 TYR H 0.93 57.2734375 0.0
115 115 SER E 0.78 26.189302444458008 0.0
161 161 TYR E 1.0 6.247583866119385 0.0
175 175 SER H 1.0 0.0 0.0
196 196 TYR H 1.0 58.879146575927734 0.0
203 203 SER C 0.37 86.32686614990234 0.0
271 271 SER H 0.78 69.03278350830078 0.0
399 399 SER H 1.0 3.081389904022217 0.0
3ZOZ A X-ray 1.9500000476837158 Monomer [ADP]A:1422 0.025190765 4, 57, 62, 76, 115, 161, 175, 196, 203, 271, 399
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 4 SER C 1.0 109.81443786621094 0.0
57 57 SER E 0.86 0.0 0.0
62 62 SER C 1.0 0.0 0.0
76 76 TYR H 0.93 61.87494659423828 0.0
115 115 SER E 0.78 27.634384155273438 0.0
161 161 TYR E 1.0 5.9326276779174805 0.0
175 175 SER H 1.0 0.0 0.0
196 196 TYR H 1.0 59.0474739074707 0.0
203 203 SER C 0.37 87.70845794677734 0.0
271 271 SER H 0.78 69.35108184814453 0.0
399 399 SER H 1.0 3.0445749759674072 0.0
2X15 A X-ray 2.0999999046325684 Monomer [ADP]A:1419 0.020176869 4, 57, 62, 76, 115, 161, 175, 196, 203, 271, 399
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 4 SER C 1.0 117.52922821044922 0.0
57 57 SER E 0.86 0.0 0.0
62 62 SER C 1.0 0.0 0.0
76 76 TYR H 0.93 68.18949890136719 0.0
115 115 SER E 0.78 28.824058532714844 0.0
161 161 TYR E 1.0 5.926290035247803 0.0
175 175 SER H 1.0 0.0 0.0
196 196 TYR H 1.0 57.11606216430664 0.0
203 203 SER C 0.37 87.76688385009766 0.0
271 271 SER H 0.78 69.86796569824219 0.0
399 399 SER H 1.0 3.337545156478882 0.0
5NP8 A X-ray 1.899999976158142 Monomer [3PG]A:505 0.08383881 57, 62, 76, 115, 161, 175, 196, 203, 271, 399
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
57 57 SER E 0.86 0.0 0.0
62 62 SER C 1.0 0.0 0.0
76 76 TYR C 0.93 54.98220443725586 0.0
115 115 SER E 0.78 28.732702255249023 0.0
161 161 TYR E 1.0 5.474621772766113 0.0
175 175 SER H 1.0 0.0 0.0
196 196 TYR H 1.0 59.39958953857422 0.0
203 203 SER C 0.37 67.42256164550781 0.0
271 271 SER H 0.78 66.68415069580078 0.0
399 399 SER H 1.0 0.0 0.0
2WZB A X-ray 1.4700000286102295 Monomer [ADP]A:1419 0.028408
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 SER C 1.0 117.28640747070312 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR H 0.93 57.066593170166016 0.0
115 114 SER E 0.78 27.82576560974121 0.0
161 160 TYR E 1.0 6.560013771057129 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 58.39748001098633 0.0
203 202 SER C 0.37 86.9212646484375 0.0
271 270 SER H 0.78 68.46134948730469 0.0
399 398 SER H 1.0 3.0435116291046143 0.0
2WZC A X-ray 1.5 Monomer [ADP]A:1420 0.027511654
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 SER C 1.0 113.67581176757812 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR H 0.93 59.96649932861328 0.0
115 114 SER E 0.78 28.448427200317383 0.0
161 160 TYR E 1.0 6.405678749084473 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 57.90810012817383 0.0
203 202 SER C 0.37 86.74882507324219 0.0
271 270 SER H 0.78 68.55325317382812 0.0
399 398 SER H 1.0 2.9234619140625 0.0
2WZD A X-ray 1.559999942779541 Monomer [ADP]A:1420 0.025900034
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 SER C 1.0 110.5545883178711 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR H 0.93 57.77176284790039 0.0
115 114 SER E 0.78 29.44416046142578 0.0
161 160 TYR E 1.0 6.714348793029785 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 59.178993225097656 0.0
203 202 SER C 0.37 76.28472900390625 0.0
271 270 SER H 0.78 67.65483856201172 0.0
399 398 SER H 1.0 3.3811416625976562 0.0
5M1R A X-ray 1.6399999856948853 Monomer [MG]A:503 0.029583873
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
2 1 SER C 1.0 98.71709442138672 0.0
4 3 SER H 1.0 75.57203674316406 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.12117308378219604 0.0
76 75 TYR H 0.93 45.10517501831055 0.0
115 114 SER E 0.78 30.130027770996094 0.0
161 160 TYR E 1.0 2.8175981044769287 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 57.64169692993164 0.0
203 202 SER C 0.37 63.72845458984375 0.0
271 270 SER H 0.78 65.1607437133789 0.0
399 398 SER H 1.0 0.0 0.0
5M6Z A X-ray 1.6699999570846558 Monomer [3PG]A:501 0.018310172
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
2 1 SER C 1.0 98.87881469726562 0.0
4 3 SER C 1.0 77.8312759399414 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.14553771913051605 0.0
76 75 TYR C 0.93 56.08317947387695 0.0
115 114 SER E 0.78 29.117877960205078 0.0
161 160 TYR E 1.0 3.4371585845947266 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 59.535091400146484 0.0
203 202 SER C 0.37 69.23072814941406 0.0
271 270 SER H 0.78 60.02227783203125 0.0
399 398 SER H 1.0 0.0 0.0
2XE6 A X-ray 1.7400000095367432 Monomer [3PG]A:1417 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR H 0.93 54.17232131958008 0.0
115 114 SER E 0.78 27.09158706665039 0.0
161 160 TYR E 1.0 6.247025966644287 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 64.96256256103516 0.0
203 202 SER C 0.37 71.5372543334961 0.0
271 270 SER H 0.78 68.84225463867188 0.0
399 398 SER H 1.0 0.0 0.0
2XE8 A X-ray 1.7899999618530273 Monomer [3PG]A:1417 0.07727185
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR H 0.93 49.62669372558594 0.0
115 114 SER E 0.78 27.392438888549805 0.0
161 160 TYR E 1.0 5.438137054443359 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 65.28599548339844 0.0
203 202 SER C 0.37 65.86654663085938 0.0
271 270 SER H 0.78 63.94809341430664 0.0
399 398 SER H 1.0 0.0 0.0
3C3B A X-ray 1.7999999523162842 Monomer [PO4]A:417 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
2 1 SER C 1.0 118.90676879882812 0.0
4 3 SER C 1.0 109.3658447265625 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR C 0.93 46.40165710449219 0.0
115 114 SER E 0.78 25.8760929107666 0.0
161 160 TYR E 1.0 6.102926731109619 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 73.53868103027344 0.0
203 202 SER C 0.37 57.92744064331055 0.0
271 270 SER H 0.78 64.77804565429688 0.0
399 398 SER H 1.0 0.6691580414772034 0.0
5M3U A X-ray 1.809999942779541 Monomer [ADP]A:501 0.024504626
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
2 1 SER C 1.0 96.05538177490234 0.0
4 3 SER C 1.0 81.27977752685547 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR C 0.93 54.165000915527344 0.0
115 114 SER E 0.78 23.723356246948242 0.0
161 160 TYR E 1.0 4.381882667541504 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 55.637420654296875 0.0
203 202 SER C 0.37 69.84465789794922 0.0
271 270 SER H 0.78 63.61538314819336 0.0
399 398 SER H 1.0 0.0 0.0
3C39 A X-ray 1.850000023841858 Monomer [3PG]A:417 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
2 1 SER C 1.0 113.79994201660156 0.0
4 3 SER C 1.0 106.93487548828125 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR C 0.93 52.93389129638672 0.0
115 114 SER E 0.78 27.7999324798584 0.0
161 160 TYR E 1.0 5.477699279785156 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 67.5920181274414 0.0
203 202 SER C 0.37 58.721012115478516 0.0
271 270 SER H 0.78 63.078521728515625 0.0
399 398 SER H 1.0 0.0 0.0
2YBE A X-ray 2.0 Monomer [LA8]A:1419 0.027569791
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 SER C 1.0 120.1261215209961 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR H 0.93 64.92668151855469 0.0
115 114 SER E 0.78 30.984865188598633 0.0
161 160 TYR E 1.0 5.318295955657959 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 59.985172271728516 0.0
203 202 SER C 0.37 82.25440216064453 0.0
271 270 SER H 0.78 73.49229431152344 0.0
399 398 SER H 1.0 4.040634632110596 0.0
2ZGV A X-ray 2.0 Monomer [ADP]A:417 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 SER C 1.0 65.22745513916016 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.12287786602973938 0.0
76 75 TYR C 0.93 35.294559478759766 0.0
115 114 SER E 0.78 23.48178482055664 0.0
161 160 TYR E 1.0 2.5060932636260986 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 56.27267837524414 0.0
203 202 SER C 0.37 67.08615112304688 0.0
271 270 SER H 0.78 44.89462661743164 0.0
399 398 SER H 1.0 0.0 0.0
5MXM A X-ray 2.049999952316284 Monomer [3PG]A:502 0.034732904
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 SER C 1.0 117.3932876586914 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR H 0.93 63.13983154296875 0.0
115 114 SER E 0.78 27.51548957824707 0.0
161 160 TYR E 1.0 6.559969902038574 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 60.00148010253906 0.0
203 202 SER C 0.37 87.29635620117188 0.0
271 270 SER H 0.78 72.21676635742188 0.0
399 398 SER H 1.0 1.792373538017273 0.0
4O33 A X-ray 2.0999999046325684 Monomer [3PG]A:502 0.05548058
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
2 1 SER C 1.0 25.92706298828125 0.0
4 3 SER C 1.0 98.69861602783203 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR C 0.93 50.54655456542969 0.0
115 114 SER E 0.78 26.598222732543945 0.0
161 160 TYR E 1.0 4.657750129699707 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 66.4776840209961 0.0
203 202 SER C 0.37 72.00211334228516 0.0
271 270 SER H 0.78 67.61868286132812 0.0
399 398 SER H 1.0 1.0725853443145752 0.0
2XE7 A X-ray 2.200000047683716 Monomer [3PG]A:1417 0.05132729
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR C 0.93 47.25695037841797 0.0
115 114 SER E 0.78 32.036949157714844 0.0
161 160 TYR E 1.0 4.835680961608887 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 60.00294876098633 0.0
203 202 SER C 0.37 66.33426666259766 0.0
271 270 SER H 0.78 70.63459777832031 0.0
399 398 SER H 1.0 0.0 0.0
3C3A A X-ray 2.299999952316284 Monomer [3PG]A:417 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 SER C 1.0 36.27417755126953 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR H 0.93 50.69921875 0.0
115 114 SER E 0.78 25.217336654663086 0.0
161 160 TYR E 1.0 5.320240020751953 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 74.97420501708984 0.0
203 202 SER C 0.37 67.65287780761719 0.0
271 270 SER H 0.78 59.491214752197266 0.0
399 398 SER H 1.0 0.0 0.0
3C3C A X-ray 2.4000000953674316 Monomer [3PG]A:418 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
2 1 SER C 1.0 107.6191635131836 0.0
4 3 SER C 1.0 109.57744598388672 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR C 0.93 51.80463790893555 0.0
115 114 SER E 0.78 28.330303192138672 0.0
161 160 TYR E 1.0 5.008224964141846 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 74.02854919433594 0.0
203 202 SER C 0.37 58.974159240722656 0.0
271 270 SER H 0.78 61.383758544921875 0.0
399 398 SER H 1.0 0.16729053854942322 0.0
2Y3I A X-ray 2.9000000953674316 Monomer [CL]A:1417 0.025162116
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
4 3 SER C 1.0 108.19447326660156 0.0
57 56 SER E 0.86 0.0 0.0
62 61 SER C 1.0 0.0 0.0
76 75 TYR C 0.93 71.55144500732422 0.0
115 114 SER E 0.78 29.453170776367188 0.0
161 160 TYR E 1.0 6.717916965484619 0.0
175 174 SER H 1.0 0.0 0.0
196 195 TYR H 1.0 60.26747131347656 0.0
203 202 SER C 0.37 74.68910217285156 0.0
271 270 SER H 0.78 63.631771087646484 0.0
399 398 SER H 1.0 4.962135314941406 0.0

Mutations

Showing 11 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
88 L P Disease Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]
158 G V Disease Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]
164 D V Disease Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]
206 R P Disease Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]
252 E A Disease Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]
266 V M Disease Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]
268 D N Polymorphism
285 D V Disease Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]
315 D N Disease Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]
316 C R Disease Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]
352 T N Polymorphism