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 A1 |
Enzyme Information
| 2.5.1.18 |
Glutathione transferase.
based on mapping to UniProt P08263
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.- |
Peroxidases.
based on mapping to UniProt P08263
|
| 5.3.3.- |
Transposing C=C bonds.
based on mapping to UniProt P08263
|
UniProtKB Entries (1)
| P08263 |
GSTA1_HUMAN
Homo sapiens
Glutathione S-transferase A1
|
PDB Structure
| PDB | 1PL2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix.
Acta Crystallogr.,Sect.D
|
