CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.390 | Enolase-like; domain 1 |
|
3.30.390.30 | FAD/NAD-linked reductase, C-terminal dimerisation domain |
Domain Context
CATH Clusters
| Superfamily | 3.30.390.30 |
| Functional Family | Glutathione reductase |
Enzyme Information
| 1.8.1.7 |
Glutathione-disulfide reductase.
based on mapping to UniProt P00390
2 glutathione + NADP(+) = glutathione disulfide + NADPH.
-!- Activity is dependent on a redox-active disulfide in each of the active centers. -!- Formerly EC 1.6.4.2.
|
UniProtKB Entries (1)
| P00390 |
GSHR_HUMAN
Homo sapiens
Glutathione reductase, mitochondrial
|
PDB Structure
| PDB | 1GRT |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
Biochemistry
|
