6F66
Crystal structure of glutathione transferase Omega 3S from Trametes versicolor in complex with 2,4-Dihydroxybenzophenone
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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue CUT A 300 |
| Chain | Residue |
| A | PRO16 |
| A | TYR17 |
| A | ASN120 |
| A | PHE123 |
| A | ARG124 |
| A | TRP127 |
| A | PHE168 |
| A | ARG171 |
| A | HOH406 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | ALA89 |
| A | ASP90 |
| A | ARG105 |
| A | HOH417 |
| A | HOH429 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue GSH A 302 |
| Chain | Residue |
| A | SER15 |
| A | TYR17 |
| A | LYS54 |
| A | LYS55 |
| A | ILE56 |
| A | PRO57 |
| A | GLU80 |
| A | SER81 |
| A | HOH442 |
| A | HOH522 |
| B | ASN117 |
| B | TYR118 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 303 |
| Chain | Residue |
| A | MET142 |
| A | GLY145 |
| A | ALA146 |
| B | PRO52 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 304 |
| Chain | Residue |
| A | PRO52 |
| A | HOH543 |
| A | HOH565 |
| B | MET142 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CUT B 300 |
| Chain | Residue |
| B | PRO16 |
| B | TYR17 |
| B | PHE123 |
| B | TRP127 |
| B | PHE168 |
| B | HOH427 |
| B | HOH448 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 301 |
| Chain | Residue |
| B | ALA89 |
| B | ASP90 |
| B | ARG105 |
| B | HOH450 |
| B | HOH478 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 302 |
| Chain | Residue |
| A | HOH422 |
| B | GLY145 |
| B | HOH419 |
| B | HOH579 |
| B | HOH611 |
| site_id | AC9 |
| 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 | HOH422 |
| B | HOH544 |
