3KRR

Crystal Structure of JAK2 complexed with a potent quinoxaline ATP site inhibitor

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	21
Details	BINDING SITE FOR RESIDUE DQX A 1

Chain	Residue
A	HOH83
A	GLU930
A	TYR931
A	LEU932
A	PRO933
A	TYR934
A	GLY935
A	ARG980
A	ASN981
A	LEU983
A	GLU987
A	HOH84
A	GLY993
A	ASP994
A	HOH88
A	HOH142
A	LEU855
A	GLY856
A	GLY858
A	ALA880
A	MET929

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVEmCrydplqdntgevv.....AVKK

Chain	Residue	Details
A	LEU855-LYS883

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

Chain	Residue	Details
A	TYR972-VAL984

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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	ASP976

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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	LEU855
A	LYS882

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site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q62120

Chain	Residue	Details
A	TYR868
A	TYR966
A	TYR972

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16174768

Chain	Residue	Details
A	PTR1007

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:16174768

Chain	Residue	Details
A	PTR1008

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