3NYX

Non-phosphorylated TYK2 JH1 domain with Quinoline-Thiadiazole-Thiophene Inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein 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	11
Details	BINDING SITE FOR RESIDUE TZ1 A 1

Chain	Residue
A	PHE908
A	PHE1042
A	GLY1043
A	LYS930
A	ILE960
A	TYR962
A	LEU976
A	MET978
A	GLU979
A	VAL981
A	ASP1041

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DTT A 1184

Chain	Residue
A	GLN1005
A	ARG1136
A	CYS1142

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DTT A 2

Chain	Residue
A	CYS936
A	HIS940
A	TRP944
A	PRO991
A	ARG992

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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. LGEGHFGKVSlYcydptndgtgem......VAVK

Chain	Residue	Details
A	LEU903-LYS930

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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	ASN1023

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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	LEU903
A	LYS930

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20478313, ECO:0000269|PubMed:8702790

Chain	Residue	Details
A	TYR1054

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8702790

Chain	Residue	Details
A	TYR1055

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