2Y6O

Crystal structure of EphA4 kinase domain in complex with Dasatinib.

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 PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 1N1 A 1892

Chain	Residue
A	VAL609
A	MET702
A	GLU703
A	GLY705
A	SER763
A	HOH2298
A	HOH2299
A	HOH2300
A	ILE627
A	ALA651
A	LYS653
A	MET674
A	ILE697
A	THR699
A	GLU700
A	TYR701

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE627-LYS653

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

Chain	Residue	Details
A	TYR742-VAL754

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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	ASP746

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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	ILE627
A	LYS653

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000255

Chain	Residue	Details
A	TYR779

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