6F68
Crystal structure glutathione transferase Omega 3S from Trametes versicolor in complex with 2,4,4'-trihydroxybenzophenone
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 | 0019852 | biological_process | L-ascorbic acid metabolic process |
A | 0045174 | molecular_function | glutathione dehydrogenase (ascorbate) activity |
A | 0046872 | molecular_function | metal ion binding |
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 | 0019852 | biological_process | L-ascorbic acid metabolic process |
B | 0045174 | molecular_function | glutathione dehydrogenase (ascorbate) activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue 4EU A 301 |
Chain | Residue |
A | PHE123 |
A | TRP127 |
A | PHE128 |
A | PHE168 |
A | MET172 |
A | LEU236 |
A | GSH302 |
A | HOH404 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue GSH A 302 |
Chain | Residue |
A | TYR17 |
A | LYS54 |
A | LYS55 |
A | ILE56 |
A | PRO57 |
A | GLU80 |
A | SER81 |
A | 4EU301 |
A | HOH425 |
A | HOH508 |
B | ASN117 |
B | TYR118 |
A | SER15 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue PEG A 303 |
Chain | Residue |
A | MET142 |
A | GLY145 |
A | ALA146 |
B | PRO52 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue GOL A 304 |
Chain | Residue |
A | ALA89 |
A | ASP90 |
A | ARG105 |
A | HOH408 |
A | HOH422 |
A | HOH473 |
B | ARG105 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue PG4 B 301 |
Chain | Residue |
A | PRO52 |
B | MET142 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue 4EU B 302 |
Chain | Residue |
B | TYR17 |
B | PHE123 |
B | TRP127 |
B | PHE128 |
B | PHE168 |
B | MET172 |
B | TYR175 |
B | GSH303 |
B | HOH401 |
B | HOH443 |
site_id | AC7 |
Number of Residues | 13 |
Details | binding site for residue GSH B 303 |
Chain | Residue |
A | ASN117 |
A | TYR118 |
B | PHE14 |
B | SER15 |
B | TYR17 |
B | LYS54 |
B | LYS55 |
B | ILE56 |
B | PRO57 |
B | GLU80 |
B | SER81 |
B | 4EU302 |
B | HOH428 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CA B 304 |
Chain | Residue |
A | HOH401 |
B | GLY145 |
B | HOH497 |
B | HOH542 |
B | HOH545 |
B | HOH560 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue GOL B 305 |
Chain | Residue |
A | ARG105 |
B | ALA89 |
B | ASP90 |
B | ARG105 |
B | HOH404 |
B | HOH412 |
B | HOH482 |