5XTN
Crystal structure of baculoviral sulfhydryl oxidase P33 (C155A, C158A mutant)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016972 | molecular_function | thiol oxidase activity |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0042025 | cellular_component | host cell nucleus |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016972 | molecular_function | thiol oxidase activity |
| B | 0030430 | cellular_component | host cell cytoplasm |
| B | 0042025 | cellular_component | host cell nucleus |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016972 | molecular_function | thiol oxidase activity |
| C | 0030430 | cellular_component | host cell cytoplasm |
| C | 0042025 | cellular_component | host cell nucleus |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016972 | molecular_function | thiol oxidase activity |
| D | 0030430 | cellular_component | host cell cytoplasm |
| D | 0042025 | cellular_component | host cell nucleus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue FAD A 301 |
| Chain | Residue |
| A | ARG10 |
| A | TYR162 |
| A | MET222 |
| A | HIS225 |
| A | ASN226 |
| A | ILE228 |
| A | ASN229 |
| A | LYS232 |
| A | GLN235 |
| A | MET247 |
| A | TYR252 |
| A | PHE106 |
| A | ILE109 |
| A | TRP110 |
| A | MET113 |
| A | HIS114 |
| A | MET157 |
| A | ALA158 |
| A | HIS161 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue FAD B 301 |
| Chain | Residue |
| B | ARG10 |
| B | PHE106 |
| B | THR107 |
| B | ILE109 |
| B | TRP110 |
| B | HIS114 |
| B | MET157 |
| B | ALA158 |
| B | HIS161 |
| B | TYR162 |
| B | MET222 |
| B | HIS225 |
| B | ASN226 |
| B | ILE228 |
| B | ASN229 |
| B | LYS232 |
| B | GLN235 |
| B | ARG236 |
| B | MET247 |
| B | TYR252 |
| B | HOH401 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue FAD C 301 |
| Chain | Residue |
| B | ASP75 |
| C | ARG10 |
| C | PHE106 |
| C | THR107 |
| C | ILE109 |
| C | TRP110 |
| C | MET113 |
| C | HIS114 |
| C | PHE150 |
| C | MET157 |
| C | ALA158 |
| C | HIS161 |
| C | TYR162 |
| C | MET222 |
| C | HIS225 |
| C | ASN226 |
| C | ILE228 |
| C | ASN229 |
| C | LYS232 |
| C | GLN235 |
| C | ARG236 |
| C | MET247 |
| C | TYR252 |
| C | HOH403 |
| C | HOH415 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue FAD D 301 |
| Chain | Residue |
| A | ASP75 |
| D | ARG10 |
| D | PHE106 |
| D | THR107 |
| D | ILE109 |
| D | TRP110 |
| D | MET113 |
| D | HIS114 |
| D | MET157 |
| D | ALA158 |
| D | HIS161 |
| D | TYR162 |
| D | MET222 |
| D | HIS225 |
| D | ASN226 |
| D | ILE228 |
| D | ASN229 |
| D | LYS232 |
| D | GLN235 |
| D | ARG236 |
| D | MET247 |
| D | HOH407 |
