5FPY
Structure of hepatitis C virus (HCV) full-length NS3 complex with small-molecule ligand 5-bromo-1-methyl-1H-indole-2-carboxylic acid (AT21457) in an alternate binding site.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004386 | molecular_function | helicase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0019087 | biological_process | symbiont-mediated transformation of host cell |
| B | 0004386 | molecular_function | helicase activity |
| B | 0005524 | molecular_function | ATP binding |
| 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 R2N B 1721 |
| Chain | Residue |
| B | SER370 |
| B | LYS371 |
| B | VAL432 |
| B | HOH2200 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE R2N A 1721 |
| Chain | Residue |
| A | SER370 |
| A | LYS371 |
| A | VAL432 |
| A | GLN434 |
| A | HOH2403 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8861916 |
| Chain | Residue | Details |
| A | HIS57 | |
| A | ASP81 | |
| B | HIS57 | |
| B | ASP81 |
| 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:0000269|PubMed:8861916, ECO:0000269|PubMed:9568891 |
| Chain | Residue | Details |
| A | SER139 | |
| B | SER139 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916, ECO:0000269|PubMed:9568891 |
| Chain | Residue | Details |
| A | CYS97 | |
| A | CYS99 | |
| B | CYS97 | |
| B | CYS99 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916 |
| Chain | Residue | Details |
| A | CYS145 | |
| A | HIS149 | |
| B | CYS145 | |
| B | HIS149 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541 |
| Chain | Residue | Details |
| A | ALA204 | |
| B | ALA204 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9WMX2 |
| Chain | Residue | Details |
| A | SER211 | |
| A | GLU291 | |
| B | SER211 | |
| B | GLU291 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by serine protease/helicase NS3 => ECO:0000250|UniProtKB:P27958 |
| Chain | Residue | Details |
| A | THR631 | |
| B | THR631 |
