1GSD

GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM

Summary for 1GSD

• Entry DOI: 10.2210/pdb1gsd/pdb
• Descriptor: GLUTATHIONE TRANSFERASE A1-1 (2 entities in total)
• Functional Keywords: transferase (glutathione)
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P08263
• Total number of polymer chains: 4
• Total formula weight: 102155.70

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

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)