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6CU6

Crystal structure of GMPPNP-bound G12R mutant of human KRAS4b

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 Residues5
Detailsbinding site for residue MG A 401
ChainResidue
ASER17
ATHR35
AGNP402
AHOH519
AHOH541

site_idAC2
Number of Residues26
Detailsbinding site for residue GNP A 402
ChainResidue
ALYS16
ASER17
AALA18
APHE28
AVAL29
AASP30
AGLU31
ATYR32
ATHR35
AGLY60
AASN116
ALYS117
AASP119
ALEU120
ASER145
AALA146
AMG401
AHOH519
AHOH527
AHOH541
AHOH553
AHOH568
AARG12
AGLY13
AVAL14
AGLY15

site_idAC3
Number of Residues5
Detailsbinding site for residue MG B 401
ChainResidue
BSER17
BTHR35
BGNP403
BHOH501
BHOH528

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL B 402
ChainResidue
AARG149
BASP33
BASP38
BTYR40

site_idAC5
Number of Residues26
Detailsbinding site for residue GNP B 403
ChainResidue
BARG12
BGLY13
BVAL14
BGLY15
BLYS16
BSER17
BALA18
BPHE28
BVAL29
BASP30
BGLU31
BTYR32
BTHR35
BALA59
BASN116
BLYS117
BASP119
BLEU120
BSER145
BALA146
BLYS147
BMG401
BHOH501
BHOH522
BHOH528
BHOH533

site_idAC6
Number of Residues4
Detailsbinding site for residue MG C 401
ChainResidue
CSER17
CASP57
CGNP402
CHOH530

site_idAC7
Number of Residues19
Detailsbinding site for residue GNP C 402
ChainResidue
CARG12
CGLY13
CVAL14
CGLY15
CLYS16
CSER17
CALA18
CPHE28
CVAL29
CASN116
CLYS117
CASP119
CLEU120
CSER145
CALA146
CLYS147
CMG401
CHOH530
CHOH545

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsMotif: {"description":"Effector region"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues47
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 Residues3
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 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_FI5
Number of Residues3
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

243083

PDB entries from 2025-10-15

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