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4LYF

Crystal Structure of small molecule vinylsulfonamide 8 covalently bound to K-Ras G12C

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007165biological_processsignal transduction
B0016020cellular_componentmembrane
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
C0007165biological_processsignal transduction
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP A 201
ChainResidue
AGLY13
AASN116
ALYS117
AASP119
ALEU120
ASER145
AALA146
ALYS147
AHOH317
AHOH323
AHOH328
AVAL14
AHOH330
AHOH346
AGLY15
ALYS16
ASER17
AALA18
APHE28
AVAL29
AASP30

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 21C B 201
ChainResidue
BVAL9
BGLY10
BCYS12
BLYS16
BTHR58
BGLU62
BARG68
BTYR71
BMET72
BTYR96
BHOH356
BHOH362
CARG73

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GDP B 202
ChainResidue
BGLY13
BVAL14
BGLY15
BLYS16
BSER17
BALA18
BPHE28
BASN116
BLYS117
BASP119
BLEU120
BSER145
BALA146
BLYS147
BHOH322
BHOH326
BHOH334
BHOH342
BHOH358

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP C 201
ChainResidue
CGLY13
CVAL14
CGLY15
CLYS16
CSER17
CALA18
CPHE28
CALA59
CASN116
CLYS117
CASP119
CLEU120
CSER145
CALA146
CLYS147
CHOH304
CHOH313
CHOH328
CHOH331
CHOH335

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22431598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22566140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34380736","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N-acetylmethionine; in GTPase KRas; alternate","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"N-acetylthreonine; in GTPase KRas, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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