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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
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BBL A 901
ChainResidue
AALA6
AHOH906
AHOH908
AHOH1062
AHOH1149
ALEU8
AARG10
AARG97
AGLN101
AHIS102
APRO127
AMET128
ALEU129

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACE A 306
ChainResidue
AGLY170
AMET171
ACYS172
AVAL307

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE VAL A 307
ChainResidue
AVAL28
AMET29
APRO169
AGLY170
ACYS172
AACE306
ANFA308
AHOH909
AHOH919

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NFA A 308
ChainResidue
AVAL28
AASN124
APRO169
AGLY170
AVAL307
AHOH915
AHOH1042
AHOH1086

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"For protease 3C activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16288920","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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