CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.1050 | Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2 |
|
1.20.1050.10 |
Domain Context
CATH Clusters
| Superfamily | 1.20.1050.10 |
| Functional Family | Glutathione S-transferase omega-1 |
Enzyme Information
| 2.5.1.18 |
Glutathione transferase.
based on mapping to UniProt P78417
RX + glutathione = HX + R-S-glutathione.
-!- A group of enzymes of broad specificity. -!- R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. -!- Also catalyzes the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange. -!- Formerly EC 1.8.6.1, EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14 and EC 4.4.1.7.
|
| 1.20.4.2 |
Methylarsonate reductase.
based on mapping to UniProt P78417
Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H(2)O.
-!- The product, methylarsonite, is biologically methylated by EC 2.1.1.137 to form cacodylic acid. -!- Formerly EC 1.97.1.7.
|
| 1.8.5.1 |
Glutathione dehydrogenase (ascorbate).
based on mapping to UniProt P78417
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.
|
UniProtKB Entries (1)
| P78417 |
GSTO1_HUMAN
Homo sapiens
Glutathione S-transferase omega-1
|
PDB Structure
| PDB | 3LFL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Novel folding and stability defects cause a deficiency of human glutathione transferase omega 1.
J.Biol.Chem.
|
