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 Mu 5 |
Enzyme Information
| 2.5.1.18 |
Glutathione transferase.
based on mapping to UniProt P41043
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.
|
| 1.11.1.9 |
Glutathione peroxidase.
based on mapping to UniProt P41043
2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O.
-!- Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 on phospholipids, can act as acceptor, but more slowly than H(2)O(2) (cf. EC 1.11.1.12).
|
UniProtKB Entries (1)
| P41043 |
GSTS1_DROME
Drosophila melanogaster
Glutathione S-transferase S1
|
PDB Structure
| PDB | 1M0U |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of a Drosophila Sigma Class Glutathione S-transferase Reveals a Novel
Active Site Topography Suited for Lipid Peroxidation Products
J.Mol.Biol.
|
