5XTP
Crystal structure of baculoviral sulfhydryl oxidase P33 (H227A 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 | 24 |
Details | binding site for residue FAD A 301 |
Chain | Residue |
A | ARG10 |
A | HIS161 |
A | TYR162 |
A | MET222 |
A | HIS225 |
A | ASN226 |
A | ILE228 |
A | ASN229 |
A | LYS232 |
A | GLN235 |
A | ARG236 |
A | PHE106 |
A | MET247 |
A | TYR252 |
A | HOH405 |
A | HOH407 |
A | HOH419 |
A | THR107 |
A | ILE109 |
A | TRP110 |
A | HIS114 |
A | PHE151 |
A | MET157 |
A | CYS158 |
site_id | AC2 |
Number of Residues | 24 |
Details | binding site for residue FAD B 301 |
Chain | Residue |
B | ARG10 |
B | PHE106 |
B | THR107 |
B | ILE109 |
B | TRP110 |
B | HIS114 |
B | PHE151 |
B | MET157 |
B | CYS158 |
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 | HOH413 |
B | HOH415 |
B | HOH420 |
site_id | AC3 |
Number of Residues | 26 |
Details | binding site for residue FAD C 301 |
Chain | Residue |
A | ASP75 |
C | PHE106 |
C | THR107 |
C | ILE109 |
C | TRP110 |
C | MET113 |
C | HIS114 |
C | VAL149 |
C | PHE150 |
C | CYS158 |
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 | HOH402 |
C | HOH403 |
C | HOH406 |
C | HOH418 |
site_id | AC4 |
Number of Residues | 27 |
Details | binding site for residue FAD D 301 |
Chain | Residue |
D | HOH434 |
D | HOH435 |
B | ASP75 |
D | ARG10 |
D | PHE106 |
D | THR107 |
D | ILE109 |
D | TRP110 |
D | MET113 |
D | HIS114 |
D | VAL149 |
D | PHE150 |
D | CYS158 |
D | HIS161 |
D | TYR162 |
D | MET222 |
D | HIS225 |
D | ASN226 |
D | ILE228 |
D | ASN229 |
D | LYS232 |
D | GLN235 |
D | ARG236 |
D | MET247 |
D | TYR252 |
D | HOH406 |
D | HOH421 |