6X8G

Crystal structure of TYK2 with Compound 22

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	19
Details	binding site for residue UWM A 4000

Chain	Residue
A	LEU903
A	TYR980
A	VAL981
A	PRO982
A	GLY984
A	ARG1027
A	ASN1028
A	LEU1030
A	GLY1040
A	ASP1041
A	HOH4173
A	GLY904
A	GLU905
A	GLY906
A	GLY909
A	VAL911
A	ALA928
A	LYS930
A	GLU979

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

Chain	Residue	Details
A	TYR1019-LEU1031

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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	ASP1023

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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	LYS930
A	LEU903

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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	PTR1054

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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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