2OC0
Structure of NS3 complexed with a ketoamide inhibitor SCh491762
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 |
| C | 0006508 | biological_process | proteolysis |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0019087 | biological_process | symbiont-mediated transformation of host cell |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 901 |
| Chain | Residue |
| A | CYS97 |
| A | CYS99 |
| A | CYS145 |
| A | HOH1000 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 902 |
| Chain | Residue |
| C | CYS97 |
| C | CYS99 |
| C | CYS145 |
| C | HOH915 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 801 |
| Chain | Residue |
| A | ILE17 |
| A | THR38 |
| A | CYS16 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HU1 A 999 |
| Chain | Residue |
| A | GLN41 |
| A | HIS57 |
| A | ILE132 |
| A | LYS136 |
| A | GLY137 |
| A | SER138 |
| A | SER139 |
| A | PHE154 |
| A | ARG155 |
| A | ALA156 |
| A | ALA157 |
| A | CYS159 |
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_FI5 |
| 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 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 22 |
| Details | Region: {"description":"NS3-binding","evidences":[{"source":"PubMed","id":"7769699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8861917","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 |
| C | ASP81 | |
| C | SER139 | |
| C | GLY137 | |
| C | HIS57 |
| site_id | MCSA1 |
| Number of Residues | |
| 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 | |
| Details | M-CSA 776 |
| Chain | Residue | Details |
| C | HIS57 | proton shuttle (general acid/base) |
| C | ASP81 | electrostatic stabiliser |
| C | GLY137 | electrostatic stabiliser |
| C | SER139 | covalently attached, electrostatic stabiliser |
