1GSF

GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID

Summary for 1GSF

Entry DOI	10.2210/pdb1gsf/pdb
Descriptor	GLUTATHIONE TRANSFERASE A1-1, ETHACRYNIC ACID (3 entities in total)
Functional Keywords	a1-1, transferase (glutathione)
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm: P08263
Total number of polymer chains	4
Total formula weight	103368.25
Authors	L'Hermite, G.,Sinning, I.,Cameron, A.D.,Jones, T.A. (deposition date: 1995-06-09, release date: 1995-09-15, Last modification date: 2024-02-07)
Primary citation	Cameron, A.D.,Sinning, I.,L'Hermite, G.,Olin, B.,Board, P.G.,Mannervik, B.,Jones, T.A. Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Structure, 3:717-727, 1995 Cited by PubMed Abstract: Glutathione transferases (GSTs) constitute a family of isoenzymes that catalyze the conjugation of the tripeptide glutathione with a wide variety of hydrophobic compounds bearing an electrophilic functional group. Recently, a number of X-ray structures have been reported which have defined both the glutathione- and the substrate-binding sites in these enzymes. The structure of the glutathione-free enzyme from a mammalian source has not, however, been reported previously. PubMed: 8591048 DOI: 10.1016/S0969-2126(01)00206-4 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation