6BQK
CRYSTAL STRUCTURE OF HEPATIS C VIRUS PROTEASE (NS3) COMPLEXED WITH TRIPEPTIDIC ACYL SULFONAMIDE INHIBITOR (COMPOUND 18)
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 | 22 |
| Details | binding site for residue Z1E A 301 |
| Chain | Residue |
| A | GLN41 |
| A | SER138 |
| A | SER139 |
| A | PHE154 |
| A | ARG155 |
| A | ALA156 |
| A | ALA157 |
| A | ASP168 |
| A | HOH407 |
| A | HOH452 |
| B | TYR6 |
| A | PHE43 |
| B | ALA7 |
| B | GLN8 |
| B | HOH436 |
| A | HIS57 |
| A | VAL78 |
| A | ASP81 |
| A | ARG123 |
| A | LEU135 |
| A | LYS136 |
| A | GLY137 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | CYS97 |
| A | CYS99 |
| A | CYS145 |
| A | HIS149 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue Z1E B 301 |
| Chain | Residue |
| A | TYR6 |
| A | ALA7 |
| A | GLN8 |
| A | GLU30 |
| B | PHE43 |
| B | HIS57 |
| B | VAL78 |
| B | ASP81 |
| B | ARG123 |
| B | LEU135 |
| B | LYS136 |
| B | GLY137 |
| B | SER139 |
| B | PHE154 |
| B | ARG155 |
| B | ALA156 |
| B | ALA157 |
| B | ASP168 |
| B | HOH430 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | CYS97 |
| B | CYS99 |
| B | CYS145 |
| B | HIS149 |
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":"8386278","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8861917","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":"8861917","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"},{"source":"PubMed","id":"8248148","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8386278","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8861917","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21507982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1N1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RGQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A4R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2F9V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O8M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OBQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OC0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OC1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OC8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OIN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21507982","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RGQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A4R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2F9V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O8M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OBQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OC0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OC1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OC8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OIN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21507982","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 776 |
| Chain | Residue | Details |
| A | HIS57 | proton shuttle (general acid/base) |
| A | ASP81 | electrostatic stabiliser |
| A | GLY137 | electrostatic stabiliser |
| A | SER139 | covalently attached, electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 776 |
| Chain | Residue | Details |
| B | HIS57 | proton shuttle (general acid/base) |
| B | ASP81 | electrostatic stabiliser |
| B | GLY137 | electrostatic stabiliser |
| B | SER139 | covalently attached, electrostatic stabiliser |
