18GS
GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE
Summary for 18GS
| Entry DOI | 10.2210/pdb18gs/pdb |
| Descriptor | GLUTATHIONE S-TRANSFERASE, GLUTATHIONE S-(2,4 DINITROBENZENE), 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total) |
| Functional Keywords | glutathione transferase, dinitrobenzyl-glutathione, detoxification, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 48092.84 |
| Authors | Oakley, A.J.,Lo Bello, M.,Ricci, G.,Federici, G.,Parker, M.W. (deposition date: 1997-12-07, release date: 1999-01-13, Last modification date: 2024-05-22) |
| Primary citation | Oakley, A.J.,Lo Bello, M.,Nuccetelli, M.,Mazzetti, A.P.,Parker, M.W. The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site). J.Mol.Biol., 291:913-926, 1999 Cited by PubMed Abstract: Glutathione S -transferases (GSTs) play a pivotal role in the detoxification of foreign chemicals and toxic metabolites. They were originally termed ligandins because of their ability to bind large molecules (molecular masses >400 Da), possibly for storage and transport roles. The location of the ligandin site in mammalian GSTs is still uncertain despite numerous studies in recent years. Here we show by X-ray crystallography that the ligandin binding site in human pi class GST P1-1 occupies part of one of the substrate binding sites. This work has been extended to the determination of a number of enzyme complex crystal structures which show that very large ligands are readily accommodated into this substrate binding site and in all, but one case, causes no significant movement of protein side-chains. Some of these molecules make use of a hitherto undescribed binding site located in a surface pocket of the enzyme. This site is conserved in most, but not all, classes of GSTs suggesting it may play an important functional role. PubMed: 10452896DOI: 10.1006/jmbi.1999.3029 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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