CATH Domain 4edyB01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.30	Glutaredoxin
	3.40.30.10	Glutaredoxin

Domain Context

CATH Clusters

Superfamily	Glutaredoxin
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	4EDY
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Investigation of the binding pocket of human hematopoietic prostaglandin (PG) D2 synthase (hH-PGDS): a tale of two waters. Trujillo, J.I., Kiefer, J.R., Huang, W., Day, J.E., Moon, J., Jerome, G.M., Bono, C.P., Kornmeier, C.M., Williams, M.L., Kuhn, C., Rennie, G.R., Wynn, T.A., Carron, C.P., Thorarensen, A. Bioorg.Med.Chem.Lett.