3MJ2

X-ray crystal structure of ITK complexed with inhibitor BMS-509744

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	0004715	molecular_function	non-membrane spanning protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE MJG A 1

Chain	Residue
A	ILE369
A	MET438
A	GLU439
A	GLY441
A	CYS442
A	ARG486
A	ASN487
A	LEU489
A	SER499
A	ASP500
A	HOH1131
A	SER371
A	HOH4016
A	GLY372
A	VAL377
A	ALA389
A	LYS391
A	GLU405
A	GLU436
A	PHE437

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	23
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGQFGLVHlGywlnkdk...........VAIK

Chain	Residue	Details
A	ILE369-LYS391

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

Chain	Residue	Details
A	VAL478-VAL490

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP482

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE369
A	LYS391

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by LCK => ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	TYR512

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	SER565

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