2O8M
Crystal structure of the S139A mutant of Hepatitis C Virus NS3/4A protease
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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 201 |
| Chain | Residue |
| A | CYS97 |
| A | CYS99 |
| A | CYS145 |
| A | HOH1116 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 201 |
| Chain | Residue |
| B | CYS97 |
| B | CYS99 |
| B | CYS145 |
| B | HOH292 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 1001 |
| Chain | Residue |
| A | HOH1022 |
| C | LEU231 |
| C | GLY233 |
| C | HOH1002 |
| A | THR4 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1002 |
| Chain | Residue |
| A | ALA5 |
| A | ALA111 |
| A | HOH1008 |
| A | HOH1024 |
| B | HOH246 |
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 | 1 |
| Details | Site: {"description":"Cleavage; by protease NS2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01030","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| 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 | ALA139 | |
| 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 | ALA139 | |
| B | GLY137 | |
| B | 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 | ALA139 | covalently attached, electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | |
| Details | M-CSA 776 |
| Chain | Residue | Details |
| B | HIS57 | proton shuttle (general acid/base) |
| B | ASP81 | electrostatic stabiliser |
| B | GLY137 | electrostatic stabiliser |
| B | ALA139 | covalently attached, electrostatic stabiliser |
