4B6E
Discovery of an allosteric mechanism for the regulation of HCV NS3 protein function
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 | transformation of host cell by virus |
| 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 | transformation of host cell by virus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1721 |
| Chain | Residue |
| A | THR254 |
| A | GLY255 |
| A | THR269 |
| A | HOH2084 |
| A | HOH2186 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1721 |
| Chain | Residue |
| B | LYS210 |
| B | SER211 |
| B | THR212 |
| B | THR206 |
| B | GLY207 |
| B | SER208 |
| B | GLY209 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 10L B 1722 |
| Chain | Residue |
| B | VAL78 |
| B | ASP81 |
| B | MET485 |
| B | VAL524 |
| B | CYS525 |
| B | GLN526 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| 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_FI4 |
| 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_FI5 |
| 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_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541 |
| Chain | Residue | Details |
| A | ALA204 | |
| B | ALA204 |
| site_id | SWS_FT_FI7 |
| 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_FI8 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by serine protease/helicase NS3 => ECO:0000250|UniProtKB:P27958 |
| Chain | Residue | Details |
| A | THR631 | |
| B | THR631 |
