1LJR

GLUTATHIONE TRANSFERASE (HGST T2-2) FROM HUMAN

Summary for 1LJR

• Entry DOI: 10.2210/pdb1ljr/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE, GLUTATHIONE (2 entities in total)
• Functional Keywords: transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 55690.56

Authors

Rossjohn, J.,Mckinstry, W.J.,Oakley, A.J.,Verger, D.,Flanagan, J.,Chelvanayagam, G.,Tan, K.L.,Board, P.G.,Parker, M.W. (deposition date: 1998-03-08, release date: 1999-03-23, Last modification date: 2024-04-03)

Primary citation

Rossjohn, J.,McKinstry, W.J.,Oakley, A.J.,Verger, D.,Flanagan, J.,Chelvanayagam, G.,Tan, K.L.,Board, P.G.,Parker, M.W.
Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site.
Structure, 6:309-322, 1998

PubMed Abstract: Glutathione S-transferases (GSTs) comprise a multifunctional group of enzymes that play a critical role in the cellular detoxification process. These enzymes reduce the reactivity of toxic compounds by catalyzing their conjugation with glutathione. As a result of their role in detoxification, GSTs have been implicated in the development of cellular resistance to antibiotics, herbicides and clinical drugs and their study is therefore of much interest. In mammals, the cytosolic GSTs can be divided into five distinct classes termed alpha, mu, pi, sigma and theta. The human theta class GST, hGST T2-2, possesses several distinctive features compared to GSTs of other classes, including a long C-terminal extension and a specific sulfatase activity. It was hoped that the determination of the structure of hGST T2-2 may help us to understand more about this unusual class of enzymes.

PubMed: 9551553
DOI: 10.1016/S0969-2126(98)00034-3

Experimental method

X-RAY DIFFRACTION (3.2 Å)