8FE9

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	27
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGSFGVVRrGewdapsgktvs.......VAVK

Chain	Residue	Details
A	LEU132-LYS158

---

site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNLLL

Chain	Residue	Details
A	PHE248-LEU260

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	259
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	9
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified 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"}]}

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Details

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