4K8B
Crystal structure of HCV NS3/4A protease complexed with inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003724 | molecular_function | RNA helicase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019028 | cellular_component | viral capsid |
| A | 0019062 | biological_process | virion attachment to host cell |
| A | 0019087 | biological_process | symbiont-mediated transformation of host cell |
| A | 0033644 | cellular_component | host cell membrane |
| A | 0043657 | cellular_component | host cell |
| A | 0044423 | cellular_component | virion component |
| A | 0046718 | biological_process | symbiont entry into host cell |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0055036 | cellular_component | virion membrane |
| B | 0003724 | molecular_function | RNA helicase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019028 | cellular_component | viral capsid |
| B | 0019062 | biological_process | virion attachment to host cell |
| B | 0019087 | biological_process | symbiont-mediated transformation of host cell |
| B | 0033644 | cellular_component | host cell membrane |
| B | 0043657 | cellular_component | host cell |
| B | 0044423 | cellular_component | virion component |
| B | 0046718 | biological_process | symbiont entry into host cell |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0055036 | cellular_component | virion membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 201 |
| Chain | Residue |
| A | CYS97 |
| A | THR98 |
| A | CYS99 |
| A | CYS145 |
| A | HOH306 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 1RR A 202 |
| Chain | Residue |
| A | ASP81 |
| A | ARG123 |
| A | VAL132 |
| A | LEU135 |
| A | LYS136 |
| A | GLY137 |
| A | SER138 |
| A | SER139 |
| A | PHE154 |
| A | ARG155 |
| A | ALA156 |
| A | ALA157 |
| A | CYS159 |
| A | ASP168 |
| A | HOH345 |
| B | VAL78 |
| B | 1RR202 |
| A | TYR56 |
| A | HIS57 |
| A | VAL78 |
| A | ASP79 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 203 |
| Chain | Residue |
| A | ARG11 |
| A | GLY15 |
| A | ASN27 |
| B | ARG11 |
| B | GLY15 |
| B | ASN27 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 204 |
| Chain | Residue |
| A | LEU21 |
| A | ARG24 |
| A | LYS26 |
| A | HOH331 |
| B | GLN9 |
| B | GLY12 |
| B | LEU13 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 201 |
| Chain | Residue |
| B | CYS97 |
| B | THR98 |
| B | CYS99 |
| B | CYS145 |
| B | HOH325 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 1RR B 202 |
| Chain | Residue |
| A | TYR56 |
| A | ASP79 |
| A | 1RR202 |
| B | TYR56 |
| B | HIS57 |
| B | ASP79 |
| B | ASP81 |
| B | ARG123 |
| B | VAL132 |
| B | LEU135 |
| B | LYS136 |
| B | GLY137 |
| B | SER138 |
| B | SER139 |
| B | PHE154 |
| B | ARG155 |
| B | ALA156 |
| B | ALA157 |
| B | CYS159 |
| B | HOH302 |
| B | HOH314 |
| B | HOH316 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 203 |
| Chain | Residue |
| A | GLY12 |
| A | LEU13 |
| A | LEU14 |
| B | ARG24 |
| B | LYS26 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 301 |
| Chain | Residue |
| A | GLN28 |
| A | GLU30 |
| B | GLN28 |
| C | ARG228 |
| D | ARG228 |
