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2CXV

Dual Modes of Modification of Hepatitis A Virus 3C Protease by a Serine-Derived betaLactone: Selective Crystallization and High-resolution Structure of the His-102 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
AHOH932
AHOH992
AHOH1007
AHOH1106
ALEU8
AARG10
AARG97
AGLN101
AHIS102
APRO127
AMET128
ALEU129

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

242842

PDB entries from 2025-10-08

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