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6V6F

Crystal structure of Q61L KRAS(GMPPNP)-NF1(GRD)-SPRED1(EVH1) complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0043087biological_processregulation of GTPase activity
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
C0007165biological_processsignal transduction
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue ZN A 201
ChainResidue
AHIS49
ACYS55

site_idAC2
Number of Residues1
Detailsbinding site for residue FMT A 202
ChainResidue
AARG110

site_idAC3
Number of Residues2
Detailsbinding site for residue FMT B 1601
ChainResidue
BLYS1419
CGLN70

site_idAC4
Number of Residues24
Detailsbinding site for residue GNP C 501
ChainResidue
CSER17
CALA18
CPHE28
CVAL29
CASP30
CGLU31
CTYR32
CPRO34
CTHR35
CGLY60
CASN116
CLYS117
CASP119
CLEU120
CSER145
CALA146
CLYS147
CMG502
CHOH603
CHOH604
CGLY13
CVAL14
CGLY15
CLYS16

site_idAC5
Number of Residues6
Detailsbinding site for residue MG C 502
ChainResidue
CSER17
CTHR35
CASP57
CGNP501
CHOH603
CHOH604

site_idAC6
Number of Residues1
Detailsbinding site for residue FMT C 503
ChainResidue
CTYR137

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 Residues1
DetailsSite: {"description":"Arginine finger; crucial for GTP hydrolysis by stabilizing the transition state","evidences":[{"source":"PROSITE-ProRule","id":"PRU00167","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsMotif: {"description":"Effector region"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
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_FI4
Number of Residues1
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_FI5
Number of Residues1
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_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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