1W3C
Crystal structure of the Hepatitis C Virus NS3 Protease in complex with a peptidomimetic inhibitor
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 | 10 |
| Details | Binding site for Ligand DN1 A1176 bound to SER A 139 |
| Chain | Residue |
| A | HIS57 |
| A | CYS159 |
| A | LYS136 |
| A | GLY137 |
| A | SER138 |
| A | SER139 |
| A | PHE154 |
| A | ARG155 |
| A | ALA156 |
| A | ALA157 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | Binding site for Ligand DN2 B1176 bound to SER B 139 |
| Chain | Residue |
| B | HIS57 |
| B | LEU135 |
| B | LYS136 |
| B | GLY137 |
| B | SER138 |
| B | SER139 |
| B | ARG155 |
| B | ALA156 |
| B | ALA157 |
| B | HOH2087 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical => ECO:0000250|UniProtKB:P27958 |
| Chain | Residue | Details |
| A | VAL55-TYR75 | |
| B | VAL55-TYR75 |
| 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:8389908, ECO:0000305|PubMed:8392606, ECO:0000305|PubMed:9060645 |
| Chain | Residue | Details |
| A | HIS57 | |
| B | HIS57 |
| 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:0000305|PubMed:8389908, ECO:0000305|PubMed:8392606 |
| Chain | Residue | Details |
| A | ASP81 | |
| B | ASP81 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166 |
| Chain | Residue | Details |
| A | SER139 | |
| B | SER139 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:9060645 |
| Chain | Residue | Details |
| A | CYS97 | |
| A | CYS99 | |
| A | CYS145 | |
| A | HIS149 | |
| B | CYS97 | |
| B | CYS99 | |
| B | CYS145 | |
| B | HIS149 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by host signal peptidase => ECO:0000269|PubMed:1648221 |
| Chain | Residue | Details |
| A | ASP79 | |
| B | ASP79 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000250|UniProtKB:P27958 |
| Chain | Residue | Details |
| A | ALA1 | |
| B | ALA1 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (Hex...) threonine; by host => ECO:0000305|PubMed:23242014 |
| Chain | Residue | Details |
| A | ASP81 | |
| B | ASP81 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | CARBOHYD: O-linked (Hex...) threonine; by host => ECO:0000269|PubMed:23242014 |
| Chain | Residue | Details |
| A | ARG92 | |
| A | PHE169 | |
| B | ARG92 | |
| B | PHE169 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | CARBOHYD: O-linked (Hex...) serine; by host => ECO:0000269|PubMed:23242014 |
| Chain | Residue | Details |
| A | CYS97 | |
| A | GLY100 | |
| B | CYS97 | |
| B | GLY100 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine; by host => ECO:0000250|UniProtKB:P27958 |
| Chain | Residue | Details |
| A | VAL113 | |
| A | ARG119 | |
| A | LEU126 | |
| A | LEU144 | |
| B | VAL113 | |
| B | ARG119 | |
| B | LEU126 | |
| B | LEU144 |
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 |
