5FPT
Structure of hepatitis C virus (HCV) full-length NS3 complex with small-molecule ligand 2-(1-methyl-1H-indol-3-yl)acetic acid (AT3437) 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 | 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 | 7 |
Details | BINDING SITE FOR RESIDUE 3VY A 1721 |
Chain | Residue |
A | THR254 |
A | GLY255 |
A | THR269 |
A | GLY271 |
A | LYS272 |
A | TYR502 |
A | HOH2138 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 3VY B 1721 |
Chain | Residue |
B | GLY255 |
B | THR269 |
B | ALA275 |
B | TYR502 |
B | HOH2181 |
B | VAL232 |
B | THR254 |
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 |