2A4O

Dual modes of modification of Hepatitis A virus 3C protease by a serine derived beta-lactone: selective crytstallization and high resolution structure of the His102 adduct

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004197	molecular_function	cysteine-type endopeptidase activity
A	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE BBL A 901

Chain	Residue
A	ALA6
A	HOH906
A	HOH908
A	HOH1062
A	HOH1149
A	LEU8
A	ARG10
A	ARG97
A	GLN101
A	HIS102
A	PRO127
A	MET128
A	LEU129

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACE A 306

Chain	Residue
A	GLY170
A	MET171
A	CYS172
A	VAL307

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site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE VAL A 307

Chain	Residue
A	VAL28
A	MET29
A	PRO169
A	GLY170
A	CYS172
A	ACE306
A	NFA308
A	HOH909
A	HOH919

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site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NFA A 308

Chain	Residue
A	VAL28
A	ASN124
A	PRO169
A	GLY170
A	VAL307
A	HOH915
A	HOH1042
A	HOH1086

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: For protease 3C activity => ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000269|PubMed:16288920

Chain	Residue	Details
A	HIS44
A	ASP84
A	CYS172

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Cleavage; by protease 3C => ECO:0000250|UniProtKB:P08617

Chain	Residue	Details
A	GLN219

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