3VQS
Crystal structure of HCV NS5B RNA polymerase with a novel piperazine inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| A | 0039694 | biological_process | viral RNA genome replication |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| B | 0039694 | biological_process | viral RNA genome replication |
| C | 0003723 | molecular_function | RNA binding |
| C | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| C | 0039694 | biological_process | viral RNA genome replication |
| D | 0003723 | molecular_function | RNA binding |
| D | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| D | 0039694 | biological_process | viral RNA genome replication |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE JT1 A 1000 |
| Chain | Residue |
| A | VAL179 |
| A | CYS289 |
| A | ASN316 |
| A | SER368 |
| A | LEU384 |
| A | MET414 |
| A | TYR415 |
| A | ILE447 |
| A | TYR448 |
| A | TYR452 |
| A | ILE454 |
| A | TYR191 |
| A | ILE462 |
| A | LEU466 |
| A | LEU547 |
| A | PHE551 |
| A | HOH3109 |
| A | HOH3130 |
| A | GLY192 |
| A | PHE193 |
| A | TYR195 |
| A | SER196 |
| A | PRO197 |
| A | ARG200 |
| A | SER288 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE JT1 B 601 |
| Chain | Residue |
| B | VAL179 |
| B | TYR191 |
| B | PHE193 |
| B | TYR195 |
| B | SER196 |
| B | PRO197 |
| B | ARG200 |
| B | SER288 |
| B | CYS289 |
| B | SER368 |
| B | LEU384 |
| B | MET414 |
| B | TYR415 |
| B | ILE447 |
| B | TYR448 |
| B | TYR452 |
| B | ILE454 |
| B | ILE462 |
| B | LEU466 |
| B | TYR555 |
| B | SER556 |
| B | HOH3288 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 602 |
| Chain | Residue |
| B | PRO93 |
| B | SER96 |
| B | ARG168 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE JT1 C 601 |
| Chain | Residue |
| C | VAL179 |
| C | TYR191 |
| C | GLY192 |
| C | PHE193 |
| C | TYR195 |
| C | SER196 |
| C | PRO197 |
| C | ARG200 |
| C | SER288 |
| C | CYS289 |
| C | SER368 |
| C | LEU384 |
| C | MET414 |
| C | TYR415 |
| C | ILE447 |
| C | TYR448 |
| C | TYR452 |
| C | ILE454 |
| C | ILE462 |
| C | TYR555 |
| C | SER556 |
| C | HOH3336 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 602 |
| Chain | Residue |
| C | PRO93 |
| C | SER96 |
| C | ARG168 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE JT1 D 1000 |
| Chain | Residue |
| D | HOH3294 |
| D | VAL179 |
| D | TYR191 |
| D | GLY192 |
| D | PHE193 |
| D | TYR195 |
| D | SER196 |
| D | PRO197 |
| D | ARG200 |
| D | SER288 |
| D | CYS289 |
| D | ASN316 |
| D | SER368 |
| D | LEU384 |
| D | MET414 |
| D | TYR415 |
| D | ILE447 |
| D | TYR448 |
| D | TYR452 |
| D | ILE454 |
| D | ILE462 |
| D | LEU466 |
| D | LEU547 |
| D | PHE551 |
| D | HOH3155 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:10557268, ECO:0000305|PubMed:11884572 |
| Chain | Residue | Details |
| A | ASP220 | |
| A | ASP318 | |
| A | ASP319 | |
| B | ASP220 | |
| B | ASP318 | |
| B | ASP319 | |
| C | ASP220 | |
| C | ASP318 | |
| C | ASP319 | |
| D | ASP220 | |
| D | ASP318 | |
| D | ASP319 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine; by host => ECO:0000250|UniProtKB:P26662 |
| Chain | Residue | Details |
| A | SER29 | |
| A | SER42 | |
| B | SER29 | |
| B | SER42 | |
| C | SER29 | |
| C | SER42 | |
| D | SER29 | |
| D | SER42 |
