3WD6
Crystal structure of Bombyx mori omega-class glutathione transferase in complex with GSH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0045174 | molecular_function | glutathione dehydrogenase (ascorbate) activity |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0045174 | molecular_function | glutathione dehydrogenase (ascorbate) activity |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004364 | molecular_function | glutathione transferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006749 | biological_process | glutathione metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0045174 | molecular_function | glutathione dehydrogenase (ascorbate) activity |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004364 | molecular_function | glutathione transferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006749 | biological_process | glutathione metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0045174 | molecular_function | glutathione dehydrogenase (ascorbate) activity |
| D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 304 |
| Chain | Residue |
| A | ILE10 |
| A | LEU48 |
| A | ASN49 |
| A | GLN52 |
| A | ILE53 |
| A | GLN223 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG A 305 |
| Chain | Residue |
| A | PRO110 |
| A | ASP171 |
| A | GLU174 |
| A | PRO175 |
| A | GLY176 |
| A | ARG106 |
| A | PRO107 |
| A | LEU108 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE GSH A 306 |
| Chain | Residue |
| A | CYS38 |
| A | TYR40 |
| A | LEU62 |
| A | LYS65 |
| A | ALA76 |
| A | LYS77 |
| A | VAL78 |
| A | PRO79 |
| A | GLU91 |
| A | SER92 |
| A | HOH418 |
| A | HOH478 |
| A | HOH481 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE K B 301 |
| Chain | Residue |
| A | LYS29 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE K B 302 |
| Chain | Residue |
| B | GSH304 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 303 |
| Chain | Residue |
| B | VAL168 |
| B | LEU207 |
| B | GLU210 |
| B | TYR211 |
| B | ASN214 |
| B | LYS217 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE GSH B 304 |
| Chain | Residue |
| B | CYS38 |
| B | TYR40 |
| B | LEU62 |
| B | LYS65 |
| B | LYS77 |
| B | VAL78 |
| B | PRO79 |
| B | GLU91 |
| B | SER92 |
| B | K302 |
| B | HOH409 |
| B | HOH456 |
| B | HOH468 |
| B | HOH481 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD C 301 |
| Chain | Residue |
| C | ARG243 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 304 |
| Chain | Residue |
| C | LEU23 |
| C | PRO24 |
| C | PHE26 |
| C | ARG31 |
| C | TYR33 |
| C | LYS72 |
| C | GLU82 |
| C | GLU85 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO C 305 |
| Chain | Residue |
| C | ARG18 |
| C | LYS19 |
| C | GLY20 |
| C | ASP21 |
| C | PRO66 |
| C | GLU67 |
| C | TRP68 |
| C | HOH436 |
| D | ARG18 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE GSH C 306 |
| Chain | Residue |
| C | CYS38 |
| C | TYR40 |
| C | LEU62 |
| C | LYS65 |
| C | ALA76 |
| C | LYS77 |
| C | VAL78 |
| C | PRO79 |
| C | GLU91 |
| C | SER92 |
| C | HOH405 |
| C | HOH419 |
| C | HOH421 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE K D 302 |
| Chain | Residue |
| D | LYS72 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 303 |
| Chain | Residue |
| D | MET35 |
| D | TYR37 |
| D | PHE234 |
| D | TYR238 |
| site_id | BC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GSH D 304 |
| Chain | Residue |
| D | CYS38 |
| D | TYR40 |
| D | LEU62 |
| D | LYS65 |
| D | ALA76 |
| D | LYS77 |
| D | VAL78 |
| D | PRO79 |
| D | GLU91 |
| D | SER92 |
| D | HOH422 |
| D | HOH441 |
