2OIN
crystal structure of HCV NS3-4A R155K mutant
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 901 |
| Chain | Residue |
| A | CYS123 |
| A | CYS125 |
| A | CYS171 |
| A | HOH903 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 902 |
| Chain | Residue |
| B | CYS1123 |
| B | THR1124 |
| B | CYS1125 |
| B | CYS1171 |
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 | ASP107 | |
| A | HIS83 | |
| A | SER165 | |
| A | GLY163 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rgq |
| Chain | Residue | Details |
| B | GLY1163 | |
| B | ASP1107 | |
| B | HIS1083 | |
| B | SER1165 |
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 776 |
| Chain | Residue | Details |
| A | HIS83 | proton shuttle (general acid/base) |
| A | ASP107 | electrostatic stabiliser |
| A | GLY163 | electrostatic stabiliser |
| A | SER165 | covalently attached, electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | |
| Details | M-CSA 776 |
| Chain | Residue | Details |
| B | HIS1083 | proton shuttle (general acid/base) |
| B | ASP1107 | electrostatic stabiliser |
| B | GLY1163 | electrostatic stabiliser |
| B | SER1165 | covalently attached, electrostatic stabiliser |
