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6OB2

Crystal structure of wild-type KRAS (GMPPNP-bound) in complex with GAP-related domain (GRD) of neurofibromin (NF1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
B0043087biological_processregulation of GTPase activity
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
C0007165biological_processsignal transduction
C0016020cellular_componentmembrane
D0043087biological_processregulation of GTPase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 201
ChainResidue
AASP154
AARG161
BMET1225
BALA1226
BASN1229

site_idAC2
Number of Residues26
Detailsbinding site for residue GNP A 202
ChainResidue
ALYS16
ASER17
AALA18
APHE28
AVAL29
AASP30
AGLU31
APRO34
ATHR35
AGLY60
AASN116
ALYS117
AASP119
ALEU120
ASER145
AALA146
ALYS147
AMG203
AHOH303
AHOH304
AHOH305
AHOH308
AGLY12
AGLY13
AVAL14
AGLY15

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 203
ChainResidue
ASER17
ATHR35
AGNP202
AHOH304
AHOH305

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL B 1501
ChainResidue
AMET67
AGLN70
BVAL1398
BSER1399
BLYS1409
BGLU1415
BLYS1419

site_idAC5
Number of Residues22
Detailsbinding site for residue GNP C 201
ChainResidue
CGLY12
CGLY13
CVAL14
CGLY15
CLYS16
CSER17
CALA18
CPHE28
CVAL29
CASP30
CPRO34
CTHR35
CGLY60
CASN116
CLYS117
CASP119
CSER145
CALA146
CLYS147
CMG202
CHOH301
CHOH302

site_idAC6
Number of Residues5
Detailsbinding site for residue MG C 202
ChainResidue
CSER17
CTHR35
CGNP201
CHOH301
CHOH302

Functional Information from PROSITE/UniProt
site_idPS00509
Number of Residues15
DetailsRAS_GTPASE_ACTIV_1 Ras GTPase-activating proteins (rasGAP) domain signature. SaMFLRFINPAIVSP
ChainResidueDetails
BSER1386-PRO1400

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

site_idSWS_FT_FI2
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_FI3
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_FI4
Number of Residues2
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 Residues2
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

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Arginine finger; crucial for GTP hydrolysis by stabilizing the transition state","evidences":[{"source":"PROSITE-ProRule","id":"PRU00167","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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