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7KMR

Crystal structure analysis of human KRAS mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000164cellular_componentprotein phosphatase type 1 complex
A0000165biological_processMAPK cascade
A0000166molecular_functionnucleotide binding
A0001889biological_processliver development
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005741cellular_componentmitochondrial outer membrane
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0007165biological_processsignal transduction
A0007265biological_processRas protein signal transduction
A0007565biological_processfemale pregnancy
A0008284biological_processpositive regulation of cell population proliferation
A0009629biological_processresponse to gravity
A0009898cellular_componentcytoplasmic side of plasma membrane
A0010628biological_processpositive regulation of gene expression
A0012505cellular_componentendomembrane system
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019002molecular_functionGMP binding
A0019003molecular_functionGDP binding
A0019221biological_processcytokine-mediated signaling pathway
A0030275molecular_functionLRR domain binding
A0035900biological_processresponse to isolation stress
A0043495molecular_functionprotein-membrane adaptor activity
A0044877molecular_functionprotein-containing complex binding
A0046579biological_processpositive regulation of Ras protein signal transduction
A0051384biological_processresponse to glucocorticoid
A0051385biological_processresponse to mineralocorticoid
A0051450biological_processmyoblast proliferation
A0060038biological_processcardiac muscle cell proliferation
A2000774biological_processpositive regulation of cellular senescence
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue GDP A 201
ChainResidue
AGLY13
ALEU120
ASER145
AALA146
ALYS147
AHOH312
AHOH315
AHOH325
AHOH349
AHOH382
AHOH393
AVAL14
AGLY15
ALYS16
ASER17
AALA18
AASN116
ALYS117
AASP119

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

site_idSWS_FT_FI2
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_FI3
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_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
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

site_idSWS_FT_FI6
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"30442762","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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