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
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
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 | HOH932 |
| A | HOH992 |
| A | HOH1007 |
| A | HOH1106 |
| A | LEU8 |
| A | ARG10 |
| A | ARG97 |
| A | GLN101 |
| A | HIS102 |
| A | PRO127 |
| A | MET128 |
| A | LEU129 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"For protease 3C activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16288920","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
