4E1Z

Structure of mouse Tyk-2 complexed to a 3-aminoindazole 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	19
Details	BINDING SITE FOR RESIDUE 0MX A 1201

Chain	Residue
A	ARG897
A	TYR976
A	VAL977
A	PRO978
A	GLY980
A	ARG1023
A	ASN1024
A	LEU1026
A	GLY1036
A	ASP1037
A	GLN1114
A	LEU899
A	GLY900
A	GLU901
A	GLY902
A	GLY905
A	VAL907
A	ALA924
A	GLU975

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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	LEU899-LYS926

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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	ARG1023

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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	HIS903
A	GLU930

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P29597

Chain	Residue	Details
A	ASP884

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:P29597

Chain	Residue	Details
A	ARG1054

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P29597

Chain	Residue	Details
A	GLU1055

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