1DY9
Inhibition of the Hepatitis C Virus NS3/4A Protease. The Crystal Structures of Two Protease-Inhibitor Complexes (inhibitor I)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0019087 | biological_process | symbiont-mediated transformation of host cell |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0019087 | biological_process | symbiont-mediated transformation of host cell |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 2ZF A 401 |
| Chain | Residue |
| A | SER42 |
| A | ALA157 |
| A | CYS159 |
| A | HOH2027 |
| A | HOH2098 |
| A | HIS57 |
| A | LYS136 |
| A | GLY137 |
| A | SER138 |
| A | SER139 |
| A | PHE154 |
| A | ARG155 |
| A | ALA156 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 2ZF B 401 |
| Chain | Residue |
| B | SER42 |
| B | HIS57 |
| B | VAL132 |
| B | LYS136 |
| B | GLY137 |
| B | SER138 |
| B | SER139 |
| B | PHE154 |
| B | ARG155 |
| B | ALA156 |
| B | ALA157 |
| B | HOH2102 |
| B | HOH2103 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 300 |
| Chain | Residue |
| B | CYS97 |
| B | CYS99 |
| B | CYS145 |
| B | HOH2098 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system; for serine protease NS3 activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8389908","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8392606","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9060645","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system; for serine protease NS3 activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8389908","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8392606","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system; for serine protease NS3 activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9060645","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rgq |
| Chain | Residue | Details |
| A | ASP81 | |
| A | SER139 | |
| A | GLY137 | |
| A | HIS57 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rgq |
| Chain | Residue | Details |
| B | ASP81 | |
| B | SER139 | |
| B | GLY137 | |
| B | HIS57 |
