1N1L
CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X)
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 | transformation of host cell by virus |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0019087 | biological_process | transformation of host cell by virus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 300 |
| Chain | Residue |
| A | CYS97 |
| A | CYS99 |
| A | CYS145 |
| A | HOH307 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 300 |
| Chain | Residue |
| B | CYS97 |
| B | CYS99 |
| B | CYS145 |
| B | HOH304 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TRL A 200 |
| Chain | Residue |
| A | PHE43 |
| A | HIS57 |
| A | ILE132 |
| A | LEU135 |
| A | GLY137 |
| A | SER138 |
| A | SER139 |
| A | ALA156 |
| A | ALA157 |
| A | ASP168 |
| A | HOH335 |
| A | GLN41 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917 |
| Chain | Residue | Details |
| A | GLY58 | |
| B | GLY58 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000305|PubMed:8861917 |
| Chain | Residue | Details |
| A | LEU82 | |
| B | LEU82 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| 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 | GLY140 | |
| B | GLY140 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 | THR98 | |
| A | GLY100 | |
| B | THR98 | |
| B | GLY100 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 | PRO146 | |
| B | PRO146 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982 |
| Chain | Residue | Details |
| A | ALA150 | |
| B | ALA150 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by protease NS2 => ECO:0000255|PROSITE-ProRule:PRU01030 |
| Chain | Residue | Details |
| A | ALA1 | |
| B | ALA1 |
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 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 776 |
| Chain | Residue | Details |
| A | GLY58 | proton shuttle (general acid/base) |
| A | LEU82 | electrostatic stabiliser |
| A | SER138 | electrostatic stabiliser |
| A | GLY140 | covalently attached, electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 776 |
| Chain | Residue | Details |
| B | GLY58 | proton shuttle (general acid/base) |
| B | LEU82 | electrostatic stabiliser |
| B | SER138 | electrostatic stabiliser |
| B | GLY140 | covalently attached, electrostatic stabiliser |
