3CM3

High Resolution Crystal Structure of the Vaccinia Virus Dual-Specificity Phosphatase VH1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004721	molecular_function	phosphoprotein phosphatase activity
A	0004722	molecular_function	protein serine/threonine phosphatase activity
A	0004725	molecular_function	protein tyrosine phosphatase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0006470	biological_process	protein dephosphorylation
A	0008330	molecular_function	protein tyrosine/threonine phosphatase activity
A	0016311	biological_process	dephosphorylation
A	0016791	molecular_function	phosphatase activity
A	0017017	molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity
A	0019049	biological_process	virus-mediated perturbation of host defense response
A	0030430	cellular_component	host cell cytoplasm
A	0033550	molecular_function	MAP kinase tyrosine phosphatase activity
A	0039502	biological_process	symbiont-mediated suppression of host type I interferon-mediated signaling pathway
A	0039563	biological_process	symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity
A	0043409	biological_process	negative regulation of MAPK cascade
A	0044423	cellular_component	virion component
A	0052170	biological_process	symbiont-mediated suppression of host innate immune response

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 1

Chain	Residue
A	ASP1081
A	SER1112
A	ALA1113
A	ALA1114
A	GLY1115
A	ASN1117
A	ARG1118
A	HOH1199

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME A 1174

Chain	Residue
A	GLU1156
A	ASN1157
A	HOH1251
A	HOH1391
A	ASN1117

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME A 2

Chain	Residue
A	ASN1131
A	LYS1132
A	SER1134

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000269|PubMed:1848923

Chain	Residue	Details
A	SER1112

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