Welcome to Scop3P

Search for the desired protein with Uniprot accession, protein name/keyword, ProteomeXchange ID or PDB id

Ex.: O00571, ddx3x (keyword), ATP-dependent RNA helicase DDX3X, PXD000680 or 3JRV

  • Zoom in and zoom out (both with mouse and buttons on the right top corner) to see modificationson the protein
  • Slide the chart to see other modifications (both with mouse and buttons on the right topcorner)
  • Hover on the modification to see more information and position on the structure.
PDB 
 AlphaFold
Phospho-sites

Showing 8 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
8 TYR PRIDE yes
14 THR PRIDE yes
16 SER UP, PRIDE Combined yes
26 TYR PRIDE yes
55 THR UP, PRIDE Combined yes
56 SER UP, PRIDE Combined yes
63 SER UP, PRIDE Combined yes
213 THR PRIDE yes

3D structure is not available

Display Settings

Hover over to see the values, zoom (in/out) or drag by using the mouse pointer.

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
8 6 20 3 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 7 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
PXD000612 6 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
14 6 20 9 1
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
14 11 20 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 5 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
16 6 20 11 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 7 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000612 10 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
PXD001374 5 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 5 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
16 11 20 6 15
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 37 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
PXD004252 3 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD000474 1 Simulated phosphopeptide spectral library for confident site localization Homo sapiens (Human) PARTIAL 2015-03-17 HeLa cell -
PXD004940 5 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD003531 15 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD001333 5 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD002286 22 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 56 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 -
PXD002394 19 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture -
PXD001374 2 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell -
PXD001550 7 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD004452 18 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD000612 100 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001546 3 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
26 21 32 6 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 28 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
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 -
PXD001565 1 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain
55 53 66 3 5
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 6 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000612 3 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 4 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD005366 3 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 4 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon
55 54 66 2 2
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 -
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
56 53 66 4 9
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 16 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
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 -
PXD004415 1 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte
PXD003531 35 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary 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 -
PXD001333 3 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 40 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 19 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
56 54 66 3 11
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD001060 31 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
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
PXD004415 3 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 -
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD002286 58 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD006482 2 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 54 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 -
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 3 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
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 -
63 53 66 11 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI 
PXD000612 14 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
213 210 231 4 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

Structures

Showing 21 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
4R3O E X-ray 2.5999999046325684 28 D 1.0 8, 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 TYR C 1.0 154.54612731933594 0.0
14 14 THR C 1.0 45.289493560791016 0.0
16 16 SER C 1.0 12.924337387084961 0.0
26 26 TYR H 1.0 113.11438751220703 82.3206787109375
55 55 THR C 1.0 114.44332122802734 4.536179065704346
56 56 SER C 1.0 36.708229064941406 25.531400680541992
63 63 SER H 1.0 87.84233093261719 60.74358367919922
79 79 SER E 1.0 0.0 0.0
213 213 THR C 1.0 75.84857940673828 0.0
4R67 E X-ray 2.890000104904175 28 F 1.0 8, 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 TYR C 1.0 153.02281188964844 0.0
14 14 THR C 1.0 42.825904846191406 39.79415512084961
16 16 SER C 1.0 11.602822303771973 5.075982093811035
26 26 TYR H 1.0 110.45716857910156 0.0
55 55 THR C 1.0 116.9067611694336 0.0
56 56 SER C 1.0 37.03788757324219 0.0
63 63 SER H 1.0 84.77676391601562 0.0
79 79 SER E 1.0 0.0 0.0
213 213 THR C 1.0 72.22862243652344 0.0
5T0G K EM 4.400000095367432 Monomer L 0.0 8, 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 TYR C 1.0 121.76702880859375 9.147467613220215
14 14 THR C 1.0 55.73288345336914 43.19124984741211
16 16 SER C 1.0 19.56163787841797 10.470736503601074
26 26 TYR H 1.0 138.38201904296875 0.0
55 55 THR C 1.0 124.66802978515625 0.0
56 56 SER C 1.0 37.41179656982422 0.0
63 63 SER H 1.0 59.5098762512207 0.0
79 79 SER C 1.0 0.0 0.0
213 213 THR C 1.0 51.97060775756836 0.0
5GJQ F EM 4.5 7 E 1.0 8, 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 TYR C 1.0 232.36090087890625 0.0
14 14 THR C 1.0 43.69023895263672 0.0
16 16 SER C 1.0 9.795599937438965 0.0
26 26 TYR H 1.0 110.65778350830078 78.35596466064453
55 55 THR C 1.0 114.15699005126953 4.2946038246154785
56 56 SER C 1.0 40.860443115234375 24.139495849609375
63 63 SER H 1.0 90.18289184570312 66.25568389892578
79 79 SER E 1.0 0.16873718798160553 0.0
213 213 THR C 1.0 68.40007781982422 0.0
5T0H K EM 6.800000190734863 Monomer J 0.0 8, 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 TYR C 1.0 130.16746520996094 0.0
14 14 THR C 1.0 45.296958923339844 0.0
16 16 SER C 1.0 18.73832893371582 0.0
26 26 TYR H 1.0 139.82827758789062 68.1322021484375
55 55 THR C 1.0 120.22135925292969 16.88519859313965
56 56 SER C 1.0 44.03478240966797 14.09683609008789
63 63 SER H 1.0 72.77043151855469 60.701255798339844
79 79 SER C 1.0 0.24479153752326965 0.0
213 213 THR C 1.0 41.239070892333984 0.0
5T0I K EM 8.0 Monomer L 0.0 8, 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 TYR C 1.0 135.93502807617188 7.46441125869751
14 14 THR C 1.0 70.3671646118164 61.245513916015625
16 16 SER C 1.0 12.93966293334961 7.2932353019714355
26 26 TYR H 1.0 113.44763946533203 0.0
55 55 THR C 1.0 129.19654846191406 0.0
56 56 SER C 1.0 44.52889633178711 0.0
63 63 SER C 1.0 64.13916778564453 0.0
79 79 SER C 1.0 0.0 0.0
213 213 THR C 1.0 45.68069076538086 0.0
5T0J K EM 8.0 Monomer J 0.0 8, 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 TYR C 1.0 96.53326416015625 18.397043228149414
14 14 THR C 1.0 100.41981506347656 0.0
16 16 SER C 1.0 16.85618782043457 0.0
26 26 TYR H 1.0 118.81841278076172 80.49774932861328
55 55 THR C 1.0 125.02552032470703 0.0
56 56 SER C 1.0 43.40732192993164 15.712650299072266
63 63 SER C 1.0 61.51304244995117 30.404064178466797
79 79 SER C 1.0 0.0 0.0
213 213 THR C 1.0 52.574920654296875 0.0
5LE5 D X-ray 1.7999999523162842 3 [CL]D:301 0.1 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 44.501338958740234 0.0
16 16 SER C 1.0 17.081308364868164 0.0
26 26 TYR H 1.0 108.46766662597656 0.0
55 55 THR C 1.0 111.67880249023438 0.0
56 56 SER C 1.0 39.220767974853516 0.0
63 63 SER H 1.0 82.07039642333984 0.0
79 79 SER E 1.0 1.1598944664001465 0.0
213 213 THR C 1.0 51.02126693725586 0.0
5LEY D X-ray 1.899999976158142 2 [CL]D:301 0.1 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 45.07868194580078 0.0
16 16 SER C 1.0 18.96208381652832 0.0
26 26 TYR H 1.0 112.95143127441406 0.0
55 55 THR C 1.0 111.03536224365234 0.0
56 56 SER C 1.0 38.128055572509766 0.0
63 63 SER H 1.0 81.9645767211914 0.0
79 79 SER E 1.0 1.1688969135284424 0.0
213 213 THR C 1.0 49.52311706542969 0.0
5LF4 D X-ray 1.9900000095367432 2 [CL]D:301 0.97352844 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 44.7659912109375 0.0
16 16 SER C 1.0 19.618846893310547 0.0
26 26 TYR H 1.0 109.287841796875 0.0
55 55 THR C 1.0 111.19986724853516 0.0
56 56 SER C 1.0 39.27381896972656 0.0
63 63 SER H 1.0 80.14886474609375 0.0
79 79 SER E 1.0 0.6671029329299927 0.0
213 213 THR C 1.0 51.89570617675781 0.0
5LF7 D X-ray 2.0 4 [CL]D:301 0.1 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 44.23203659057617 0.0
16 16 SER C 1.0 19.800065994262695 0.0
26 26 TYR H 1.0 110.4293441772461 0.0
55 55 THR C 1.0 108.60935974121094 0.0
56 56 SER C 1.0 39.469112396240234 0.0
63 63 SER H 1.0 83.13150787353516 0.0
79 79 SER E 1.0 1.5021311044692993 0.0
213 213 THR C 1.0 49.450401306152344 0.0
5LF1 D X-ray 2.0 4 [CL]D:301 0.1 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 45.23711013793945 0.0
16 16 SER C 1.0 19.356075286865234 0.0
26 26 TYR H 1.0 110.53105163574219 0.0
55 55 THR C 1.0 109.08030700683594 0.0
56 56 SER C 1.0 37.649993896484375 0.0
63 63 SER H 1.0 78.97605895996094 0.0
79 79 SER E 1.0 1.336187481880188 0.0
213 213 THR C 1.0 47.960235595703125 0.0
5LF6 D X-ray 2.069999933242798 3 [CL]D:301 0.1 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 45.620479583740234 0.0
16 16 SER C 1.0 18.591753005981445 0.0
26 26 TYR H 1.0 108.72953796386719 0.0
55 55 THR C 1.0 110.99723815917969 0.0
56 56 SER C 1.0 37.83040237426758 0.0
63 63 SER H 1.0 82.7881851196289 0.0
79 79 SER E 1.0 1.838687777519226 0.0
213 213 THR C 1.0 46.93364715576172 0.0
5LF3 D X-ray 2.0999999046325684 4 [CL]D:301 0.1 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 45.93596649169922 0.0
16 16 SER C 1.0 20.657310485839844 0.0
26 26 TYR H 1.0 110.17902374267578 0.0
55 55 THR C 1.0 107.9596939086914 0.0
56 56 SER C 1.0 38.698970794677734 0.0
63 63 SER H 1.0 82.00963592529297 0.0
79 79 SER E 1.0 1.1688969135284424 0.0
213 213 THR C 1.0 48.60983657836914 0.0
5LEZ D X-ray 2.190000057220459 22 C 1.0 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 44.502506256103516 0.0
16 16 SER C 1.0 17.096107482910156 0.0
26 26 TYR H 1.0 108.65680694580078 74.40587615966797
55 55 THR C 1.0 110.67158508300781 5.1552958488464355
56 56 SER C 1.0 34.93204879760742 31.5132999420166
63 63 SER H 1.0 85.55252075195312 59.189640045166016
79 79 SER E 1.0 1.0023187398910522 0.0
213 213 THR C 1.0 48.981536865234375 0.0
5LEX D X-ray 2.200000047683716 28 C 1.0 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 45.960105895996094 0.0
16 16 SER C 1.0 16.857942581176758 0.0
26 26 TYR H 1.0 110.58056640625 74.64656829833984
55 55 THR C 1.0 112.6937255859375 4.17382287979126
56 56 SER C 1.0 37.572757720947266 32.114341735839844
63 63 SER H 1.0 83.6331558227539 58.101318359375
79 79 SER E 1.0 1.336187481880188 0.0
213 213 THR C 1.0 47.17277526855469 0.0
5LF0 D X-ray 2.4100000858306885 4 [CL]D:301 0.1 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 45.21185302734375 0.0
16 16 SER C 1.0 20.256689071655273 0.0
26 26 TYR H 1.0 111.0366439819336 0.0
55 55 THR C 1.0 104.71537017822266 0.0
56 56 SER C 1.0 36.992008209228516 0.0
63 63 SER H 1.0 83.64391326904297 0.0
79 79 SER E 1.0 1.838687777519226 0.0
213 213 THR C 1.0 53.56504821777344 0.0
5A0Q E EM 3.5 Monomer D 0.0 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 79.03826904296875 0.0
16 16 SER C 1.0 15.171636581420898 0.0
26 26 TYR H 1.0 112.67867279052734 71.45023345947266
55 55 THR C 1.0 115.02220153808594 0.0
56 56 SER C 1.0 48.732177734375 28.23288917541504
63 63 SER C 1.0 90.15019989013672 51.745052337646484
79 79 SER E 1.0 1.3329569101333618 0.0
213 213 THR C 1.0 51.525901794433594 0.0
6AVO H EM 3.799999952316284 Monomer I 0.0 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 44.47995376586914 0.0
16 16 SER C 1.0 20.729312896728516 0.0
26 26 TYR H 1.0 114.46758270263672 70.4356460571289
55 55 THR C 1.0 109.78547668457031 4.168189525604248
56 56 SER C 1.0 41.93623352050781 35.8044548034668
63 63 SER C 1.0 62.13391876220703 39.544189453125
79 79 SER C 1.0 0.6326833963394165 0.0
213 213 THR C 1.0 40.33164978027344 0.0
5M32 D EM 3.799999952316284 Monomer C 0.0 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 46.19630432128906 0.0
16 16 SER C 1.0 8.402934074401855 0.0
26 26 TYR H 1.0 115.87277221679688 82.53851318359375
55 55 THR C 1.0 137.5877685546875 38.439491271972656
56 56 SER C 1.0 33.854888916015625 28.465986251831055
63 63 SER C 1.0 76.189208984375 54.226356506347656
79 79 SER C 1.0 0.0 0.0
213 213 THR C 1.0 43.25980758666992 0.0
5LN3 E EM 6.800000190734863 Monomer F 0.0 14, 16, 26, 55, 56, 63, 213
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
14 14 THR C 1.0 40.94700241088867 28.37885856628418
16 16 SER C 1.0 14.23996353149414 12.946078300476074
26 26 TYR H 1.0 136.92201232910156 0.0
55 55 THR C 1.0 135.04019165039062 0.0
56 56 SER C 1.0 51.25454330444336 0.0
63 63 SER C 1.0 99.48611450195312 0.0
79 79 SER E 1.0 9.975650787353516 0.0
213 213 THR C 1.0 46.33245086669922 0.0

Mutations

Showing 0 results

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