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8FE9

Crystal structure of Ack1 kinase K161Q mutant in complex with the selective inhibitor (R)-9b

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGSFGVVRrGewdapsgktvs.......VAVK
ChainResidueDetails
ALEU132-LYS158

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNLLL
ChainResidueDetails
APHE248-LEU260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues259
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC and autocatalysis","evidences":[{"source":"PubMed","id":"15308621","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16472662","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20333297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20623637","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20979614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21169560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21309750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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