1VCP

SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM I)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis
B	0004252	molecular_function	serine-type endopeptidase activity
B	0006508	biological_process	proteolysis
C	0004252	molecular_function	serine-type endopeptidase activity
C	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG A 272

Chain	Residue
A	CYS119
A	CYS134
A	LEU135

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG B 271

Chain	Residue
B	CYS119
B	CYS134
B	LEU135

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG C 273

Chain	Residue
C	CYS119
C	CYS134
C	LEU135

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027

Chain	Residue	Details
A	HIS145
A	ASP167
B	HIS145
B	ASP167
C	HIS145
C	ASP167

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site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027, ECO:0000269|PubMed:3553612

Chain	Residue	Details
A	SER219
B	SER219
C	SER219

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site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: Involved in dimerization of the capsid protein => ECO:0000250|UniProtKB:Q86925

Chain	Residue	Details
A	TYR193
A	ASN226
B	TYR193
B	ASN226
C	TYR193
C	ASN226

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site_id	SWS_FT_FI4
Number of Residues	3
Details	SITE: Cleavage; by autolysis => ECO:0000269|PubMed:3553612

Chain	Residue	Details
A	TRP267
B	TRP267
C	TRP267

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