EC Number   |
Reference |
|---|
   1.8.5.1 | crystal structures of isoform GSTO1 in complex with ascoric acid, to 1.7 A resolution. Ascorbic acid binds in the glutathione site, where the glutamyl moiety of GSH binds and stacks against a conserved aromatic residue, F34 |
725717 |
| 1.8.5.1 | crystal structures of isoform GSTO2-2, stabilized through site-directed mutagenesis of cysteine residues to serines and determined at 1.9 A resolution in the presence and absence of glutathione |
725717 |
| 1.8.5.1 | in complex with acetate or glycerol |
741828 |
| 1.8.5.1 | in complex with ascorbate, hanging drop vapor diffusion method, using |
743319 |
| 1.8.5.1 | isoform DHAr2 bound to glutathione, hanging drop vapor diffusion method, using 2.0 M ammonium sulfate, 0.1 M sodium acetate, pH 4.8 |
743831 |
| 1.8.5.1 | isozyme AtDHAR2, X-ray diffraction structure determination and analysis |
765156 |
| 1.8.5.1 | isozyme OsDHAR1, X-ray diffraction structure determination and analysis |
765156 |
| 1.8.5.1 | isozyme PgDHAR1, X-ray diffraction structure determination and analysis |
765156 |
| 1.8.5.1 | modeling of structure. Protein has a typical glutathione S-transferase structure containing a smaller thioredoxin-like N-terminal domain and a larger helical C-terminal domain |
725939 |
| 1.8.5.1 | native, ascorbate-bound, and glutathione-bound enzyme forms, hanging drop vapor diffusion method, using 0.15 M potassium bromide and 30% (w/v) PEG MME 2000 |
743806 |
