2OIN
crystal structure of HCV NS3-4A R155K mutant
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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 901 |
Chain | Residue |
A | CYS123 |
A | CYS125 |
A | CYS171 |
A | HOH903 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 902 |
Chain | Residue |
B | CYS1123 |
B | THR1124 |
B | CYS1125 |
B | CYS1171 |
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 |
B | HIS1083 | |
A | HIS83 |
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 | ASP107 | |
B | ASP1107 |
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 | SER165 | |
B | SER1165 |
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 | CYS123 | |
A | CYS125 | |
B | CYS1123 | |
B | CYS1125 |
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 | CYS171 | |
B | CYS1171 |
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 | HIS175 | |
B | HIS1175 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | |
Details | M-CSA 776 |
Chain | Residue | Details |
A | HIS83 | proton shuttle (general acid/base) |
A | ASP107 | electrostatic stabiliser |
A | GLY163 | electrostatic stabiliser |
A | SER165 | covalently attached, electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | |
Details | M-CSA 776 |
Chain | Residue | Details |
B | HIS1083 | proton shuttle (general acid/base) |
B | ASP1107 | electrostatic stabiliser |
B | GLY1163 | electrostatic stabiliser |
B | SER1165 | covalently attached, electrostatic stabiliser |