4H1J

Crystal structure of PYK2 with the pyrazole 13a

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	15
Details	BINDING SITE FOR RESIDUE 0YH A 701

Chain	Residue
A	LYS457
A	GLY566
A	ASP567
A	PHE568
A	ARG572
A	HOH803
A	HOH896
A	SER473
A	GLU474
A	MET478
A	VAL487
A	GLU503
A	TYR505
A	LEU556
A	LEU565

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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. LGEGFFGEVYeGvytnhkgekin.......VAVK

Chain	Residue	Details
A	LEU431-LYS457

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

Chain	Residue	Details
A	CYS545-VAL557

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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	ASP549

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:19244237, ECO:0007744|PDB:3FZP

Chain	Residue	Details
A	LEU431
A	LYS457
A	GLU503

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9QVP9

Chain	Residue	Details
A	TYR579

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by SRC, FYN and LCK => ECO:0000269|PubMed:20028775, ECO:0000269|PubMed:20381867

Chain	Residue	Details
A	TYR580

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