5TOZ

JAK3 with covalent inhibitor PF-06651600

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	14
Details	binding site for residue 7H4 A 1201

Chain	Residue
A	LEU828
A	ARG953
A	LEU956
A	HOH1307
A	HOH1442
A	HOH1464
A	GLY829
A	ALA853
A	GLU903
A	TYR904
A	LEU905
A	GLY908
A	CYS909
A	ASP912

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site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 A 1202

Chain	Residue
A	ARG911
A	HOH1370
A	HOH1383
A	HOH1400

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVElCrydplgdntgal......VAVK

Chain	Residue	Details
A	LEU828-LYS855

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

Chain	Residue	Details
A	CYS945-VAL957

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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	ASP949

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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	LEU828
A	LYS855

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18250158

Chain	Residue	Details
A	TYR904
A	TYR939

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831699

Chain	Residue	Details
A	TYR980
A	TYR981

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