16GS
GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3
Summary for 16GS
| Entry DOI | 10.2210/pdb16gs/pdb |
| Descriptor | GLUTATHIONE S-TRANSFERASE, SULFATE ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total) |
| Functional Keywords | transferase, apoenzyme, detoxification |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 47242.08 |
| Authors | Oakley, A.J.,Lo Bello, M.,Ricci, G.,Federici, G.,Parker, M.W. (deposition date: 1997-11-30, release date: 1999-01-13, Last modification date: 2024-05-22) |
| Primary citation | Oakley, A.J.,Lo Bello, M.,Ricci, G.,Federici, G.,Parker, M.W. Evidence for an induced-fit mechanism operating in pi class glutathione transferases. Biochemistry, 37:9912-9917, 1998 Cited by PubMed Abstract: Three-dimensional structures of the apo form of human pi class glutathione transferase have been determined by X-ray crystallography. The structures suggest the enzyme recognizes its substrate, glutathione, by an induced-fit mechanism. Compared to complexed forms of the enzyme, the environment around the catalytic residue, Tyr 7, remains unchanged in the apoenzyme. This observation supports the view that Tyr 7 does not act as a general base in the reaction mechanism. The observed cooperativity of the dimeric enzyme may be due to the movements of a helix that forms one wall of the active site and, in particular, to movements of a tyrosine residue that is located in the subunit interface. PubMed: 9665696DOI: 10.1021/bi980323w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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