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5WHD

Crystal structure of KRas G12V/D38P, bound to GDP

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
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
D0007165biological_processsignal transduction
D0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue GDP A 201
ChainResidue
AGLY13
ALYS117
AASP119
ALEU120
ASER145
AALA146
ALYS147
AHOH302
AHOH310
AHOH330
AHOH362
AVAL14
AGLY15
ALYS16
ASER17
AALA18
APHE28
AALA59
AASN116

site_idAC2
Number of Residues19
Detailsbinding site for residue GDP B 201
ChainResidue
BMET1
BVAL12
BGLY13
BVAL14
BGLY15
BLYS16
BSER17
BALA18
BPHE28
BALA59
BASN116
BLYS117
BASP119
BLEU120
BSER145
BALA146
BLYS147
BHOH307
BHOH370

site_idAC3
Number of Residues19
Detailsbinding site for residue GDP C 201
ChainResidue
CVAL12
CGLY13
CVAL14
CGLY15
CLYS16
CSER17
CALA18
CPHE28
CALA59
CASN116
CLYS117
CASP119
CLEU120
CSER145
CALA146
CLYS147
CHOH328
CHOH345
CHOH346

site_idAC4
Number of Residues18
Detailsbinding site for residue GDP D 201
ChainResidue
DVAL12
DGLY13
DVAL14
DGLY15
DLYS16
DSER17
DALA18
DALA59
DASN116
DLYS117
DASP119
DLEU120
DSER145
DALA146
DLYS147
DHOH312
DHOH337
DHOH351

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsMotif: {"description":"Effector region"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues54
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_FI3
Number of Residues4
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_FI4
Number of Residues4
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_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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