1AQX

GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH MEISENHEIMER COMPLEX

1AQX の概要

• エントリーDOI: 10.2210/pdb1aqx/pdb
• 分子名称: GLUTATHIONE S-TRANSFERASE, 1-(S-GLUTATHIONYL)-2,4,6-TRINITROCYCLOHEXA-2,5-DIENE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: transferase, glutathione s-transferase, class pi, transition state, transferase-substrate complex, transferase/substrate
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 95848.94

構造登録者

Prade, L.,Huber, R.,Manoharan, T.H.,Fahl, W.E.,Reuter, W. (登録日: 1997-08-03, 公開日: 1998-03-18, 最終更新日: 2024-02-07)

主引用文献

Prade, L.,Huber, R.,Manoharan, T.H.,Fahl, W.E.,Reuter, W.
Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor.
Structure, 5:1287-1295, 1997

PubMed Abstract: Glutathione S-transferases (GSTs) are detoxification enzymes, found in all aerobic organisms, which catalyse the conjugation of glutathione with a wide range of hydrophobic electrophilic substrates, thereby protecting the cell from serious damage caused by electrophilic compounds. GSTs are classified into five distinct classes (alpha, mu, pi, sigma and theta) by their substrate specificity and primary structure. Human GSTs are of interest because tumour cells show increased levels of expression of single classes of GSTs, which leads to drug resistance. Structural differences between classes of GST can therefore be utilised to develop new anti-cancer drugs. Many mutational and structural studies have been carried out on the mu and alpha classes of GST to elucidate the reaction mechanism, whereas knowledge about the pi class is still limited.

PubMed: 9351803
DOI: 10.1016/S0969-2126(97)00281-5

実験手法

X-RAY DIFFRACTION (2 Å)