2LJR

GLUTATHIONE TRANSFERASE APO-FORM FROM HUMAN

2LJR の概要

• エントリーDOI: 10.2210/pdb2ljr/pdb
• 分子名称: GLUTATHIONE S-TRANSFERASE (2 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P30712
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55075.91

構造登録者

Rossjohn, J.,Mckinstry, W.J.,Oakley, A.J.,Verger, D.,Flanagan, J.,Chelvanayagam, G.,Tan, K.L.,Board, P.G.,Parker, M.W. (登録日: 1998-03-08, 公開日: 1999-03-23, 最終更新日: 2024-02-21)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.2 Å)