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 | Hematopoietic prostaglandin D synthase |
Enzyme Information
| 2.5.1.18 |
Glutathione transferase.
based on mapping to UniProt O60760
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.
|
| 5.3.99.2 |
Prostaglandin-D synthase.
based on mapping to UniProt O60760
(5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate.
-!- Brings about the opening of the epidioxy bridge.
|
UniProtKB Entries (1)
| O60760 |
HPGDS_HUMAN
Homo sapiens
Hematopoietic prostaglandin D synthase
|
PDB Structure
| PDB | 1V40 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
First determination of the inhibitor complex structure of human hematopoietic prostaglandin D synthase.
J.Biochem.(Tokyo)
|