3RC5
Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | HOH9 |
| A | HOH17 |
| A | HOH20 |
| A | HOH47 |
| A | TYR1006 |
| A | GLN1008 |
| A | TYR1056 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2 |
| Chain | Residue |
| A | GLY990 |
| A | SER1020 |
| A | THR1038 |
| A | ALA1039 |
| A | ARG1062 |
| A | HOH151 |
| A | LYS989 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1183 |
| Chain | Residue |
| A | CYS1097 |
| A | CYS1099 |
| A | CYS1145 |
| A | HIS1149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | SITE: (Microbial infection) Cleavage; by HCV and hepatitis GB virus B NS3/4A protease complex => ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:16301520 |
| Chain | Residue | Details |
| B | CYS7 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000305|PubMed:8861917 |
| Chain | Residue | Details |
| A | ASP1081 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8248148, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917 |
| Chain | Residue | Details |
| A | ALA1139 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1A1R, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI |
| Chain | Residue | Details |
| A | CYS1097 | |
| A | CYS1099 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI |
| Chain | Residue | Details |
| A | CYS1145 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982 |
| Chain | Residue | Details |
| A | HIS1149 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by protease NS2 => ECO:0000255|PROSITE-ProRule:PRU01030 |
| Chain | Residue | Details |
| A | LEU1000 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 776 |
| Chain | Residue | Details |
| A | HIS1057 | proton shuttle (general acid/base) |
| A | ASP1081 | electrostatic stabiliser |
| A | GLY1137 | electrostatic stabiliser |
| A | ALA1139 | covalently attached, electrostatic stabiliser |
