6OVA

Crystal Structure of TYK2 with novel pyrrolidinone 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	15
Details	binding site for residue N9G A 1200

Chain	Residue
A	LEU903
A	PRO982
A	GLY984
A	ASP988
A	ARG1027
A	ASN1028
A	ASP1041
A	GLY906
A	VAL911
A	ALA928
A	LYS930
A	ILE960
A	GLU979
A	TYR980
A	VAL981

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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	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"20478313","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8702790","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8702790","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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