1DY8
Inhibition of the Hepatitis C Virus NS3/4A Protease. The Crystal Structures of Two Protease-Inhibitor Complexes (inhibitor II)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006508 | biological_process | proteolysis |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0019087 | biological_process | transformation of host cell by virus |
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 | 13 |
Details | BINDING SITE FOR RESIDUE 0F7 A 401 |
Chain | Residue |
A | HIS57 |
A | ALA157 |
A | CYS159 |
A | ASP168 |
A | HOH2043 |
A | LEU135 |
A | LYS136 |
A | GLY137 |
A | SER138 |
A | SER139 |
A | PHE154 |
A | ARG155 |
A | ALA156 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 0F7 B 401 |
Chain | Residue |
B | HIS57 |
B | ARG123 |
B | LYS136 |
B | GLY137 |
B | SER138 |
B | SER139 |
B | PHE154 |
B | ARG155 |
B | ALA156 |
B | ALA157 |
B | ASP168 |
B | HOH2018 |
B | HOH2048 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | TRANSMEM: Helical => ECO:0000250|UniProtKB:P27958 |
Chain | Residue | Details |
A | VAL55-TYR75 | |
B | VAL55-TYR75 |
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:0000305|PubMed:8389908, ECO:0000305|PubMed:8392606, ECO:0000305|PubMed:9060645 |
Chain | Residue | Details |
A | HIS57 | |
B | HIS57 |
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:0000305|PubMed:8389908, ECO:0000305|PubMed:8392606 |
Chain | Residue | Details |
A | ASP81 | |
B | ASP81 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166 |
Chain | Residue | Details |
A | SER139 | |
B | SER139 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:9060645 |
Chain | Residue | Details |
A | CYS97 | |
A | CYS99 | |
A | CYS145 | |
A | HIS149 | |
B | CYS97 | |
B | CYS99 | |
B | CYS145 | |
B | HIS149 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Cleavage; by host signal peptidase => ECO:0000269|PubMed:1648221 |
Chain | Residue | Details |
A | ASP79 | |
B | ASP79 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000250|UniProtKB:P27958 |
Chain | Residue | Details |
A | ALA1 | |
B | ALA1 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (Hex...) threonine; by host => ECO:0000305|PubMed:23242014 |
Chain | Residue | Details |
A | ASP81 | |
B | ASP81 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | CARBOHYD: O-linked (Hex...) threonine; by host => ECO:0000269|PubMed:23242014 |
Chain | Residue | Details |
A | ARG92 | |
A | PHE169 | |
B | ARG92 | |
B | PHE169 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | CARBOHYD: O-linked (Hex...) serine; by host => ECO:0000269|PubMed:23242014 |
Chain | Residue | Details |
A | CYS97 | |
A | GLY100 | |
B | CYS97 | |
B | GLY100 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine; by host => ECO:0000250|UniProtKB:P27958 |
Chain | Residue | Details |
A | VAL113 | |
A | ARG119 | |
A | LEU126 | |
A | LEU144 | |
B | VAL113 | |
B | ARG119 | |
B | LEU126 | |
B | LEU144 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rgq |
Chain | Residue | Details |
A | ASP81 | |
A | SER139 | |
A | GLY137 | |
A | HIS57 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rgq |
Chain | Residue | Details |
B | ASP81 | |
B | SER139 | |
B | GLY137 | |
B | HIS57 |