6BQK
CRYSTAL STRUCTURE OF HEPATIS C VIRUS PROTEASE (NS3) COMPLEXED WITH TRIPEPTIDIC ACYL SULFONAMIDE INHIBITOR (COMPOUND 18)
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 | 22 |
Details | binding site for residue Z1E A 301 |
Chain | Residue |
A | GLN41 |
A | SER138 |
A | SER139 |
A | PHE154 |
A | ARG155 |
A | ALA156 |
A | ALA157 |
A | ASP168 |
A | HOH407 |
A | HOH452 |
B | TYR6 |
A | PHE43 |
B | ALA7 |
B | GLN8 |
B | HOH436 |
A | HIS57 |
A | VAL78 |
A | ASP81 |
A | ARG123 |
A | LEU135 |
A | LYS136 |
A | GLY137 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 302 |
Chain | Residue |
A | CYS97 |
A | CYS99 |
A | CYS145 |
A | HIS149 |
site_id | AC3 |
Number of Residues | 19 |
Details | binding site for residue Z1E B 301 |
Chain | Residue |
A | TYR6 |
A | ALA7 |
A | GLN8 |
A | GLU30 |
B | PHE43 |
B | HIS57 |
B | VAL78 |
B | ASP81 |
B | ARG123 |
B | LEU135 |
B | LYS136 |
B | GLY137 |
B | SER139 |
B | PHE154 |
B | ARG155 |
B | ALA156 |
B | ALA157 |
B | ASP168 |
B | HOH430 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN B 302 |
Chain | Residue |
B | CYS97 |
B | CYS99 |
B | CYS145 |
B | HIS149 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917 |
Chain | Residue | Details |
A | HIS57 | |
B | HIS57 |
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:8861917 |
Chain | Residue | Details |
A | ASP81 | |
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:8248148, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917 |
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:21507982, ECO:0007744|PDB:1A1R, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI |
Chain | Residue | Details |
A | CYS97 | |
A | CYS99 | |
B | CYS97 | |
B | CYS99 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI |
Chain | Residue | Details |
A | CYS145 | |
B | CYS145 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982 |
Chain | Residue | Details |
A | HIS149 | |
B | HIS149 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 776 |
Chain | Residue | Details |
A | HIS57 | proton shuttle (general acid/base) |
A | ASP81 | electrostatic stabiliser |
A | GLY137 | electrostatic stabiliser |
A | SER139 | covalently attached, electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 776 |
Chain | Residue | Details |
B | HIS57 | proton shuttle (general acid/base) |
B | ASP81 | electrostatic stabiliser |
B | GLY137 | electrostatic stabiliser |
B | SER139 | covalently attached, electrostatic stabiliser |