1AQX
GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH MEISENHEIMER COMPLEX
Summary for 1AQX
| Entry DOI | 10.2210/pdb1aqx/pdb |
| Descriptor | GLUTATHIONE S-TRANSFERASE, 1-(S-GLUTATHIONYL)-2,4,6-TRINITROCYCLOHEXA-2,5-DIENE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total) |
| Functional Keywords | transferase, glutathione s-transferase, class pi, transition state, transferase-substrate complex, transferase/substrate |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 95848.94 |
| Authors | Prade, L.,Huber, R.,Manoharan, T.H.,Fahl, W.E.,Reuter, W. (deposition date: 1997-08-03, release date: 1998-03-18, Last modification date: 2024-02-07) |
| Primary citation | 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 Cited by 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: 9351803DOI: 10.1016/S0969-2126(97)00281-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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