CATH Domain 1eemA01

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	Glutathione S-transferase omega-1

Enzyme Information

2.5.1.18	Glutathione transferase. based on mapping to UniProt P78417 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.
1.20.4.2	Methylarsonate reductase. based on mapping to UniProt P78417 Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H(2)O. -!- The product, methylarsonite, is biologically methylated by EC 2.1.1.137 to form cacodylic acid. -!- Formerly EC 1.97.1.7.
1.8.5.1	Glutathione dehydrogenase (ascorbate). based on mapping to UniProt P78417 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.

UniProtKB Entries (1)

GSTO1_HUMAN

Homo sapiens

Glutathione S-transferase omega-1

PDB Structure

PDB	1EEM
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Identification, characterization, and crystal structure of the Omega class glutathione transferases. Board, P.G., Coggan, M., Chelvanayagam, G., Easteal, S., Jermiin, L.S., Schulte, G.K., Danley, D.E., Hoth, L.R., Griffor, M.C., Kamath, A.V., Rosner, M.H., Chrunyk, B.A., Perregaux, D.E., Gabel, C.A., Geoghegan, K.F., Pandit, J. J.Biol.Chem.