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 |