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6MTA

KRAS P34R mutant structure in complex with GTP analogue

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 Residues26
Detailsbinding site for residue GNP A 201
ChainResidue
AGLY12
AASP30
ATYR32
ATHR35
AGLY60
AASN116
ALYS117
AASP119
ALEU120
ASER145
AALA146
AGLY13
ALYS147
AMG202
AHOH310
AHOH324
AHOH327
AHOH341
CARG41
AVAL14
AGLY15
ALYS16
ASER17
AALA18
APHE28
AVAL29

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 202
ChainResidue
ASER17
ATHR35
AGNP201
AHOH310
AHOH324

site_idAC3
Number of Residues25
Detailsbinding site for residue GNP B 201
ChainResidue
BGLY12
BGLY13
BVAL14
BGLY15
BLYS16
BSER17
BALA18
BPHE28
BVAL29
BASP30
BTYR32
BARG34
BTHR35
BGLY60
BASN116
BLYS117
BASP119
BLEU120
BSER145
BALA146
BLYS147
BMG202
BHOH308
BHOH314
BHOH321

site_idAC4
Number of Residues5
Detailsbinding site for residue MG B 202
ChainResidue
BSER17
BTHR35
BGNP201
BHOH308
BHOH314

site_idAC5
Number of Residues17
Detailsbinding site for residue GNP C 201
ChainResidue
CGLY13
CVAL14
CGLY15
CLYS16
CSER17
CALA18
CPHE28
CVAL29
CASN116
CLYS117
CASP119
CLEU120
CSER145
CALA146
CLYS147
CMG202
CHOH301

site_idAC6
Number of Residues6
Detailsbinding site for residue MG C 202
ChainResidue
CSER17
CASP57
CTHR58
CGNP201
CHOH301
CHOH328

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

240971

PDB entries from 2025-08-27

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