3LXL

Structural and Thermodynamic Characterization of the TYK2 and JAK3 Kinase Domains in Complex with CP-690550 and CMP-6

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	13
Details	BINDING SITE FOR RESIDUE IZA A 1

Chain	Residue
A	HOH2
A	LEU905
A	GLY908
A	ASN954
A	LEU956
A	HOH273
A	LEU828
A	LYS830
A	VAL836
A	ALA853
A	HIS859
A	GLU903
A	TYR904

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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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