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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9BHQ

Crystal structure of KRAS G12A in a transition state mimetic complex with CYPA and RMC-7977

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
B0000413biological_processprotein peptidyl-prolyl isomerization
B0001933biological_processnegative regulation of protein phosphorylation
B0001934biological_processpositive regulation of protein phosphorylation
B0003723molecular_functionRNA binding
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005178molecular_functionintegrin binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0006457biological_processprotein folding
B0006469biological_processnegative regulation of protein kinase activity
B0006915biological_processapoptotic process
B0016018molecular_functioncyclosporin A binding
B0016020cellular_componentmembrane
B0016853molecular_functionisomerase activity
B0019076biological_processviral release from host cell
B0030168biological_processplatelet activation
B0030182biological_processneuron differentiation
B0030593biological_processneutrophil chemotaxis
B0030595biological_processleukocyte chemotaxis
B0031982cellular_componentvesicle
B0032148biological_processactivation of protein kinase B activity
B0032873biological_processnegative regulation of stress-activated MAPK cascade
B0032991cellular_componentprotein-containing complex
B0034389biological_processlipid droplet organization
B0034599biological_processcellular response to oxidative stress
B0034774cellular_componentsecretory granule lumen
B0042118biological_processendothelial cell activation
B0043410biological_processpositive regulation of MAPK cascade
B0045069biological_processregulation of viral genome replication
B0045070biological_processpositive regulation of viral genome replication
B0046790molecular_functionvirion binding
B0050714biological_processpositive regulation of protein secretion
B0051082molecular_functionunfolded protein binding
B0051092biological_processpositive regulation of NF-kappaB transcription factor activity
B0060352biological_processcell adhesion molecule production
B0061944biological_processnegative regulation of protein K48-linked ubiquitination
B0070062cellular_componentextracellular exosome
B0070527biological_processplatelet aggregation
B1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
B1903901biological_processnegative regulation of viral life cycle
B1904399molecular_functionheparan sulfate binding
B1904813cellular_componentficolin-1-rich granule lumen
B2001233biological_processregulation of apoptotic signaling pathway
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
C0007165biological_processsignal transduction
C0016020cellular_componentmembrane
D0000413biological_processprotein peptidyl-prolyl isomerization
D0001933biological_processnegative regulation of protein phosphorylation
D0001934biological_processpositive regulation of protein phosphorylation
D0003723molecular_functionRNA binding
D0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
D0005178molecular_functionintegrin binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005925cellular_componentfocal adhesion
D0006457biological_processprotein folding
D0006469biological_processnegative regulation of protein kinase activity
D0006915biological_processapoptotic process
D0016018molecular_functioncyclosporin A binding
D0016020cellular_componentmembrane
D0016853molecular_functionisomerase activity
D0019076biological_processviral release from host cell
D0030168biological_processplatelet activation
D0030182biological_processneuron differentiation
D0030593biological_processneutrophil chemotaxis
D0030595biological_processleukocyte chemotaxis
D0031982cellular_componentvesicle
D0032148biological_processactivation of protein kinase B activity
D0032873biological_processnegative regulation of stress-activated MAPK cascade
D0032991cellular_componentprotein-containing complex
D0034389biological_processlipid droplet organization
D0034599biological_processcellular response to oxidative stress
D0034774cellular_componentsecretory granule lumen
D0042118biological_processendothelial cell activation
D0043410biological_processpositive regulation of MAPK cascade
D0045069biological_processregulation of viral genome replication
D0045070biological_processpositive regulation of viral genome replication
D0046790molecular_functionvirion binding
D0050714biological_processpositive regulation of protein secretion
D0051082molecular_functionunfolded protein binding
D0051092biological_processpositive regulation of NF-kappaB transcription factor activity
D0060352biological_processcell adhesion molecule production
D0061944biological_processnegative regulation of protein K48-linked ubiquitination
D0070062cellular_componentextracellular exosome
D0070527biological_processplatelet aggregation
D1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
D1903901biological_processnegative regulation of viral life cycle
D1904399molecular_functionheparan sulfate binding
D1904813cellular_componentficolin-1-rich granule lumen
D2001233biological_processregulation of apoptotic signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG
ChainResidueDetails
BTYR48-GLY65
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues312
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed","evidences":[{"source":"PubMed","id":"25489052","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"20364129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25678563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17742","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues16
DetailsMotif: {"description":"Effector region"}
ChainResidueDetails
site_idSWS_FT_FI13
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_FI14
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_FI15
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_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
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
Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
AILE55electrostatic stabiliser, hydrogen bond donor, steric role
AGLY60polar/non-polar interaction, steric role
AGLU63electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AARG102electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
ALEU113polar/non-polar interaction, steric role
ASER122polar/non-polar interaction, steric role
AASP126polar/non-polar interaction, steric role
site_idMCSA2
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
BARG55electrostatic stabiliser, hydrogen bond donor, steric role
BPHE60polar/non-polar interaction, steric role
BGLN63electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BASN102electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BPHE113polar/non-polar interaction, steric role
BLEU122polar/non-polar interaction, steric role
BHIS126polar/non-polar interaction, steric role

239149

PDB entries from 2025-07-23

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