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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
11 SER UP Similarity
15 SER PRIDE yes
49 THR UP, PRIDE Combined yes
54 SER PRIDE yes
140 SER UP Similarity
196 THR UP, PRIDE Experimental yes
198 THR UP, PRIDE Experimental yes
331 TYR UP Similarity
339 SER UP, PRIDE Combined yes

3D structure is not available

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Phosphorylated amino acids are colored red on the inner ring.

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

Phospho peptides

Showing 10 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
15 10 22 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
49 47 57 3 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
49 49 57 1 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 -
PXD003531 4 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
54 49 57 6 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
196 194 214 3 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 11 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 6 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD003531 1 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 8 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
198 194 214 5 4
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 1 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD000612 20 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD004415 2 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
PXD004452 9 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
198 196 214 3 13
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004252 4 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD003215 6 A Novel Method for Isolating Whole Protein from Human Cranial Bone Homo sapiens (Human) COMPLETE 2016-10-05 Osteocyte,Cranium,Osteoblast -
PXD003531 30 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD002990 1 Complementary Phosphoproteomic Approaches Link IL-23R Downstream Signaling with Metabolic Adaptation in Lymphocytes Homo sapiens (Human) COMPLETE 2016-04-21 lymph node -
PXD002286 174 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD006482 10 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 46 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture
PXD004452 21 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD002394 10 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture -
PXD001550 8 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD000680 28 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
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 -
PXD004415 32 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
339 319 343 21 6
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD004415 4 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD001546 3 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD003531 135 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD005366 57 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 6 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture
PXD004452 44 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
339 321 343 19 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 38 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD005366 4 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture -
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
339 338 343 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD003531 4 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell

Structures

Showing 36 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4WB8 A X-ray 1.5499999523162842 2 I 0.37410042
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
49 48 THR E 1.0 0.8601579666137695 0.0
54 53 SER C 1.0 91.46216583251953 55.68245315551758
196 195 THR E 1.0 2.070679187774658 0.0
202 201 THR C 1.0 27.548324584960938 26.96268653869629
205 204 TYR H 1.0 14.541189193725586 5.714650630950928
331 330 TYR C 1.0 71.31073760986328 22.43014907836914
3OVV A X-ray 1.5800000429153442 2 B 0.2462195
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 115.9241714477539 0.0
49 48 THR E 1.0 0.615645170211792 0.0
54 53 SER C 1.0 88.58578491210938 27.886070251464844
140 139 SER C 1.0 57.41219711303711 0.0
196 195 THR E 1.0 3.862922430038452 0.0
202 201 THR C 1.0 27.556230545043945 26.827392578125
205 204 TYR H 1.0 15.72893238067627 5.997176647186279
331 330 TYR C 1.0 75.06593322753906 24.715290069580078
3POO A X-ray 1.600000023841858 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 113.8427505493164 0.0
49 48 THR E 1.0 0.12296320497989655 0.0
54 53 SER C 1.0 87.52351379394531 37.74410629272461
140 139 SER C 1.0 60.53639602661133 0.0
196 195 THR E 1.0 3.353165626525879 0.0
202 201 THR C 1.0 27.681495666503906 26.65986442565918
205 204 TYR H 1.0 14.603086471557617 5.57271671295166
331 330 TYR C 1.0 73.61865997314453 24.695690155029297
4WB5 A X-ray 1.6399999856948853 2 I 0.35184664
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 89.4135513305664 0.0
49 48 THR E 1.0 1.104971170425415 0.0
54 53 SER C 1.0 92.708740234375 57.49969482421875
196 195 THR E 1.0 1.484197974205017 0.0
202 201 THR C 1.0 27.49022102355957 26.13553810119629
205 204 TYR H 1.0 15.47785758972168 5.426258087158203
331 330 TYR C 1.0 71.72179412841797 21.45413589477539
3AMA A X-ray 1.75 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 69.18801879882812 0.0
49 48 THR E 1.0 0.8594793677330017 0.0
54 53 SER C 1.0 77.84215545654297 21.82485580444336
140 139 SER C 1.0 60.080284118652344 0.0
196 195 THR E 1.0 2.955653429031372 0.0
202 201 THR C 1.0 27.726734161376953 26.705053329467773
205 204 TYR H 1.0 15.015703201293945 5.277472019195557
331 330 TYR C 1.0 84.19989776611328 11.29073429107666
4UJ1 A X-ray 1.7699999809265137 2 B 0.36276752
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 98.4881362915039 0.0
49 48 THR E 1.0 3.006909132003784 0.0
54 53 SER C 1.0 85.11416625976562 0.0
140 139 SER C 1.0 60.33393096923828 0.0
196 195 THR E 1.0 2.459282636642456 0.0
202 201 THR C 1.0 27.846261978149414 26.824583053588867
205 204 TYR H 1.0 14.595486640930176 5.56849479675293
331 330 TYR C 1.0 73.83211517333984 26.899751663208008
5IZJ A X-ray 1.850000023841858 Monomer [PO4]A:402 0.015618779
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 122.1515884399414 0.0
49 48 THR E 1.0 0.9474348425865173 0.0
54 53 SER C 1.0 89.24272918701172 0.0
140 139 SER C 1.0 57.36819839477539 0.0
196 195 THR E 1.0 5.134008407592773 0.0
202 201 THR C 1.0 43.29178237915039 0.0
205 204 TYR H 1.0 10.886443138122559 0.0
331 330 TYR C 1.0 90.2051010131836 0.0
4UJ9 A X-ray 1.8700000047683716 2 B 0.35347876
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
11 10 SER C 0.36 129.17300415039062 0.0
15 14 SER H 0.8 69.33740997314453 0.0
49 48 THR E 1.0 0.6160170435905457 0.0
54 53 SER C 1.0 84.35954284667969 3.281240701675415
140 139 SER C 1.0 56.60549545288086 0.0
196 195 THR E 1.0 2.6386077404022217 0.0
202 201 THR C 1.0 26.903926849365234 25.840312957763672
205 204 TYR H 1.0 14.082947731018066 5.429039001464844
331 330 TYR C 1.0 76.37220764160156 26.430238723754883
3OWP A X-ray 1.8799999952316284 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
49 48 THR E 1.0 0.2463836371898651 0.0
54 53 SER C 1.0 87.59467315673828 20.71404457092285
140 139 SER C 1.0 60.50834274291992 0.0
196 195 THR E 1.0 3.054699659347534 0.0
202 201 THR C 1.0 30.51483154296875 29.49315071105957
205 204 TYR H 1.0 16.484378814697266 5.716068267822266
331 330 TYR C 1.0 76.53480529785156 25.89090347290039
5BX6 A X-ray 1.8899999856948853 2 [MPD]A:402 0.28387946
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 66.44662475585938 0.1526663899421692
49 48 THR E 1.0 0.6157304644584656 0.0
54 53 SER C 1.0 83.12676239013672 0.0
140 139 SER C 1.0 49.11122512817383 0.0
196 195 THR E 1.0 1.6294695138931274 0.0
202 201 THR C 1.0 29.093978881835938 0.0
205 204 TYR H 1.0 15.897160530090332 0.0
331 330 TYR C 1.0 73.91297149658203 0.0
5BX7 A X-ray 1.8899999856948853 2 B 0.34721458
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 58.65299606323242 0.0
49 48 THR E 1.0 0.4927672743797302 0.0
54 53 SER C 1.0 86.8385238647461 22.94565200805664
140 139 SER C 1.0 60.724185943603516 0.0
196 195 THR E 1.0 1.4533923864364624 0.0
202 201 THR C 1.0 29.283405303955078 27.63587760925293
205 204 TYR H 1.0 15.159856796264648 5.716866493225098
331 330 TYR C 1.0 74.17426300048828 25.544761657714844
3L9M A X-ray 1.899999976158142 2 C 0.85958976
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 63.99176788330078 0.0
49 48 THR E 1.0 5.835629463195801 0.0
54 53 SER C 1.0 80.2246322631836 17.158788681030273
140 139 SER C 1.0 67.03205871582031 0.0
196 195 THR E 1.0 2.247129201889038 0.0
202 201 THR C 1.0 28.737585067749023 27.280349731445312
205 204 TYR H 1.0 15.124539375305176 5.407368183135986
331 330 TYR C 1.0 72.88848114013672 10.294191360473633
4WB7 A X-ray 1.899999976158142 4 [ZN]A:505 0.20016943
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
49 103 THR E 1.0 0.8580290675163269 0.0
54 108 SER C 1.0 80.97061157226562 0.0
196 250 THR E 1.0 3.243276596069336 0.0
202 256 THR C 1.0 29.853731155395508 0.0
205 259 TYR H 1.0 15.610231399536133 0.0
331 385 TYR C 1.0 67.94811248779297 0.0
4UJA A X-ray 1.9299999475479126 2 B 0.34646854
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 84.13605499267578 0.0
49 48 THR E 1.0 0.49089181423187256 0.0
54 53 SER C 1.0 87.77842712402344 7.517675876617432
140 139 SER C 1.0 58.994258880615234 0.0
196 195 THR E 1.0 1.8362199068069458 0.0
202 201 THR C 1.0 26.2918758392334 25.124658584594727
205 204 TYR H 1.0 14.136201858520508 4.982531547546387
331 330 TYR C 1.0 73.103271484375 25.801469802856445
4UJB A X-ray 1.9500000476837158 2 B 0.33540997
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 63.453399658203125 0.0
49 48 THR E 1.0 0.3697187304496765 0.0
54 53 SER C 1.0 91.56319427490234 5.0077290534973145
140 139 SER C 1.0 58.41928482055664 0.0
196 195 THR E 1.0 1.7846708297729492 0.0
202 201 THR C 1.0 28.269987106323242 27.102767944335938
205 204 TYR H 1.0 15.015052795410156 5.569817066192627
331 330 TYR C 1.0 76.0448989868164 26.451797485351562
3VQH A X-ray 1.9500000476837158 Monomer [MPD]A:402 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 62.74950408935547 0.0
49 48 THR E 1.0 0.4931391775608063 0.0
54 53 SER C 1.0 86.28799438476562 0.0
140 139 SER C 1.0 59.20726013183594 0.0
196 195 THR E 1.0 0.9986028671264648 0.0
202 201 THR C 1.0 25.48465347290039 0.0
205 204 TYR H 1.0 15.568635940551758 0.0
331 330 TYR C 1.0 76.13811492919922 0.0
3AGM A X-ray 2.0 Monomer A 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 73.98751831054688 0.0
49 48 THR E 1.0 3.2038848400115967 0.0
54 53 SER C 1.0 76.24809265136719 0.0
140 139 SER C 1.0 59.723167419433594 0.0
196 195 THR E 1.0 3.548079252243042 0.0
202 201 THR C 1.0 28.443410873413086 0.0
205 204 TYR H 1.0 15.023734092712402 0.0
331 330 TYR C 1.0 73.17037200927734 2.204409599304199
3L9L A X-ray 2.0 2 C 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 76.1387939453125 0.0
49 48 THR E 1.0 3.7317862510681152 0.0
54 53 SER C 1.0 93.52339935302734 16.767332077026367
140 139 SER C 1.0 65.35330200195312 0.0
196 195 THR E 1.0 0.9932758212089539 0.0
202 201 THR C 1.0 26.690845489501953 25.211727142333984
205 204 TYR H 1.0 15.005517959594727 5.331528663635254
331 330 TYR C 1.0 73.52642059326172 10.409709930419922
3NX8 A X-ray 2.0 Monomer B 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
49 48 THR E 1.0 0.24684087932109833 0.0
54 53 SER C 1.0 35.54180908203125 13.802255630493164
140 139 SER C 1.0 57.68592834472656 0.0
196 195 THR E 1.0 4.7261152267456055 0.0
202 201 THR C 1.0 26.424589157104492 25.384889602661133
205 204 TYR H 1.0 14.358199119567871 5.404679775238037
331 330 TYR C 1.0 72.50768280029297 21.58997917175293
3OOG A X-ray 2.0 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
49 48 THR E 1.0 5.312983512878418 0.0
54 53 SER C 1.0 70.18499755859375 0.0
140 139 SER C 1.0 58.208412170410156 0.0
196 195 THR E 1.0 3.2372097969055176 0.0
202 201 THR C 1.0 27.411745071411133 25.934303283691406
205 204 TYR H 1.0 15.581446647644043 5.707522869110107
331 330 TYR C 1.0 72.476318359375 25.876062393188477
3L9N A X-ray 2.0 2 C 0.9174044
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 113.19390106201172 0.0
49 48 THR E 1.0 3.0808634757995605 0.0
54 53 SER C 1.0 97.07474517822266 31.69379425048828
140 139 SER C 1.0 58.35915756225586 0.0
196 195 THR E 1.0 1.0027462244033813 0.0
202 201 THR C 1.0 27.452119827270508 25.714754104614258
205 204 TYR H 1.0 16.084917068481445 6.340559959411621
331 330 TYR C 1.0 74.04244995117188 18.670143127441406
4UJ2 A X-ray 2.0199999809265137 2 B 0.46299034
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 119.20052337646484 0.0
49 48 THR E 1.0 0.6160170435905457 0.0
54 53 SER C 1.0 85.61001586914062 14.19706916809082
140 139 SER C 1.0 61.02348327636719 0.0
196 195 THR E 1.0 3.5284688472747803 0.0
202 201 THR C 1.0 25.600072860717773 24.578441619873047
205 204 TYR H 1.0 15.423168182373047 5.547939300537109
331 330 TYR C 1.0 74.18177795410156 26.377864837646484
3P0M A X-ray 2.0299999713897705 2 B 0.6604755
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 116.27397918701172 0.0
49 48 THR E 1.0 0.2463836371898651 0.0
54 53 SER C 1.0 87.93045043945312 17.77090835571289
140 139 SER C 1.0 59.772315979003906 0.0
196 195 THR E 1.0 3.114511728286743 0.0
202 201 THR C 1.0 27.38334083557129 25.63463592529297
205 204 TYR H 1.0 14.490490913391113 5.131058216094971
331 330 TYR C 1.0 73.81784057617188 23.588851928710938
5N23 A X-ray 2.0899999141693115 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 57.071868896484375 0.0
49 48 THR E 1.0 0.7327273488044739 0.0
54 53 SER C 1.0 80.3822250366211 19.599609375
196 195 THR E 1.0 3.119363784790039 0.0
202 201 THR C 1.0 28.50018882751465 27.47850799560547
205 204 TYR H 1.0 13.828719139099121 5.5797648429870605
331 330 TYR C 1.0 86.05532836914062 0.0
5IZF A X-ray 2.0999999046325684 4 [SO4]A:404 0.397501
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 74.6937255859375 5.96339750289917
49 48 THR E 1.0 2.3984715938568115 0.0
54 53 SER C 1.0 85.3652572631836 0.0
140 139 SER C 1.0 67.9528579711914 0.0
196 195 THR E 1.0 3.6490182876586914 0.0
202 201 THR C 1.0 32.10885238647461 0.0
205 204 TYR H 1.0 17.064350128173828 0.0
331 330 TYR C 1.0 76.31796264648438 0.0
3AGL A X-ray 2.0999999046325684 Monomer [A03]A:351 0.1
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 56.70804977416992 0.0
49 48 THR E 1.0 0.8730753660202026 0.0
54 53 SER C 1.0 82.26421356201172 16.75862693786621
140 139 SER C 1.0 47.623809814453125 0.0
196 195 THR E 1.0 1.57388436794281 0.0
202 201 THR C 1.0 25.794227600097656 15.970837593078613
205 204 TYR H 1.0 15.59893798828125 5.449763774871826
331 330 TYR C 1.0 76.62178802490234 28.439422607421875
4WB6 A X-ray 2.0999999046325684 2 I 0.3557202
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 61.58702850341797 0.0
49 48 THR E 1.0 1.5990511178970337 0.0
54 53 SER C 1.0 78.87284851074219 60.71799850463867
196 195 THR E 1.0 2.1474528312683105 0.0
202 201 THR C 1.0 36.3734016418457 35.93857955932617
205 204 TYR H 1.0 15.197816848754883 5.1568803787231445
331 330 TYR C 1.0 69.79390716552734 21.404855728149414
339 338 SER C 1.0 33.567054748535156 0.0
4AE6 A X-ray 2.0999999046325684 Monomer B 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
49 48 THR E 1.0 60.75667953491211 0.0
54 53 SER C 1.0 68.54853057861328 49.773460388183594
140 139 SER C 1.0 69.07955932617188 0.0
196 195 THR E 1.0 2.83296275138855 0.0
202 201 THR C 1.0 37.28621292114258 0.0
205 204 TYR H 1.0 22.085750579833984 0.0
2GU8 A X-ray 2.200000047683716 2 [796]A:1001 0.5300669
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 116.24974822998047 0.0
49 48 THR E 1.0 0.0 0.0
54 53 SER C 1.0 92.20598602294922 2.788011312484741
140 139 SER C 1.0 68.126708984375 0.0
196 195 THR E 1.0 4.578012943267822 0.0
202 201 THR C 1.0 24.935089111328125 0.0
205 204 TYR H 1.0 13.032041549682617 0.0
331 330 TYR C 1.0 75.26753997802734 0.0
3OXT A X-ray 2.200000047683716 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 115.63458251953125 0.0
49 48 THR E 1.0 0.3698040843009949 0.0
54 53 SER C 1.0 89.29707336425781 11.518356323242188
140 139 SER C 1.0 61.23411178588867 0.0
196 195 THR E 1.0 4.297482490539551 0.0
202 201 THR C 1.0 30.485523223876953 28.067768096923828
205 204 TYR H 1.0 16.817445755004883 5.566892623901367
331 330 TYR C 1.0 76.33213806152344 27.345699310302734
3AMB A X-ray 2.25 2 B 0.9321231
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 66.53813934326172 0.0
49 48 THR E 1.0 2.464606761932373 0.0
54 53 SER C 1.0 79.44695281982422 0.0
140 139 SER C 1.0 59.14925003051758 0.0
196 195 THR E 1.0 3.1984663009643555 0.0
202 201 THR C 1.0 30.562740325927734 29.080835342407227
205 204 TYR H 1.0 15.459402084350586 5.7230939865112305
331 330 TYR C 1.0 89.5953140258789 0.0
4AE9 A X-ray 2.299999952316284 Monomer B 0.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
49 48 THR E 1.0 64.28968811035156 0.0
54 53 SER C 1.0 70.26084899902344 38.433311462402344
196 195 THR E 1.0 4.169440269470215 0.0
202 201 THR C 1.0 40.565006256103516 0.0
205 204 TYR H 1.0 16.637012481689453 0.0
5UZK A X-ray 2.299999952316284 2 I 0.8098481
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER C 0.8 101.82005310058594 0.0
49 48 THR E 1.0 0.6144022345542908 0.0
54 53 SER C 1.0 78.75233459472656 0.0
140 139 SER C 1.0 59.078575134277344 0.0
196 195 THR E 1.0 1.9656387567520142 0.0
202 201 THR C 1.0 28.296010971069336 26.169010162353516
205 204 TYR H 1.0 15.109049797058105 4.8175225257873535
331 330 TYR C 1.0 77.38346862792969 24.726015090942383
3MVJ A X-ray 2.490000009536743 2 J 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
49 48 THR E 1.0 0.24581113457679749 0.0
54 53 SER C 1.0 88.30913543701172 64.1601791381836
140 139 SER C 1.0 51.62321090698242 0.0
196 195 THR E 1.0 2.5705456733703613 0.0
202 201 THR C 1.0 25.66652488708496 24.1841983795166
205 204 TYR H 1.0 14.83251667022705 5.896956920623779
331 330 TYR C 1.0 71.34235382080078 22.273906707763672
5J5X A X-ray 2.5999999046325684 4 [SO4]A:403 0.62107843
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
11 10 SER C 0.36 105.74317932128906 0.0
15 14 SER H 0.8 60.355499267578125 0.0
49 48 THR E 1.0 1.9919663667678833 0.0
54 53 SER C 1.0 90.92606353759766 0.0
140 139 SER C 1.0 65.47026824951172 0.0
196 195 THR E 1.0 2.6087307929992676 0.0
202 201 THR C 1.0 36.25947952270508 0.0
205 204 TYR H 1.0 15.07116413116455 0.0
331 330 TYR C 1.0 80.84636688232422 0.0
6C0U A X-ray 2.6500000953674316 2 [EE4]A:400 0.48803434
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
15 14 SER H 0.8 81.13231658935547 0.0
49 48 THR E 1.0 0.12166932225227356 0.0
54 53 SER C 1.0 87.67588806152344 29.06804656982422
140 139 SER C 1.0 69.75302124023438 0.0
196 195 THR E 1.0 2.78450083732605 0.0
202 201 THR C 1.0 32.81039810180664 0.0
205 204 TYR H 1.0 16.45346450805664 0.0
331 330 TYR C 1.0 72.07486724853516 3.846428632736206

Mutations

Showing 4 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
41 L V Polymorphism
46 R Q Polymorphism
206 L R Disease Primary pigmented nodular adrenocortical disease 4 (PPNAD4) [MIM:615830]
264 S C Polymorphism