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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP252

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	LEU132
A	LYS158

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by SRC and autocatalysis => ECO:0000269|PubMed:15308621, ECO:0000269|PubMed:16472662, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20623637, ECO:0000269|PubMed:20979614, ECO:0000269|PubMed:21169560, ECO:0000269|PubMed:21309750, ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	TYR284

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