CATH Domain 5uehA02

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	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	5UEH
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	"Inverse Drug Discovery" Strategy To Identify Proteins That Are Targeted by Latent Electrophiles As Exemplified by Aryl Fluorosulfates. Mortenson, D.E., Brighty, G.J., Plate, L., Bare, G., Chen, W., Li, S., Wang, H., Cravatt, B.F., Forli, S., Powers, E.T., Sharpless, K.B., Wilson, I.A., Kelly, J.W. J. Am. Chem. Soc.