CATH Domain 6n4eA02

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	6N4E
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	The discovery of quinoline-3-carboxamides as hematopoietic prostaglandin D synthase (H-PGDS) inhibitors. Deaton, D.N., Do, Y., Holt, J., Jeune, M.R., Kramer, H.F., Larkin, A.L., Orband-Miller, L.A., Peckham, G.E., Poole, C., Price, D.J., Schaller, L.T., Shen, Y., Shewchuk, L.M., Stewart, E.L., Stuart, J.D., Thomson, S.A., Ward, P., Wilson, J.W., Xu, T., Guss, J.H., Musetti, C., Rendina, A.R., Affleck, K., Anders, D., Hancock, A.P., Hobbs, H., Hodgson, S.T., Hutchinson, J., Leveridge, M.V., Nicholls, H., Smith, I.E.D., Somers, D.O., Sneddon, H.F., Uddin, S., Cleasby, A., Mortenson, P.N., Richardson, C., Saxty, G. Bioorg. Med. Chem.