4YH2
Glutathione Transferase E6 from Drosophila melanogaster
Summary for 4YH2
| Entry DOI | 10.2210/pdb4yh2/pdb |
| Descriptor | Glutathione S transferase E6, GLUTATHIONE (3 entities in total) |
| Functional Keywords | transferase, drosophila |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 4 |
| Total formula weight | 101399.55 |
| Authors | Wongsantichon, J.,Robinson, R.C.,Ketterman, A.J. (deposition date: 2015-02-26, release date: 2016-02-10, Last modification date: 2024-03-20) |
| Primary citation | Wongsantichon, J.,Robinson, R.C.,Ketterman, A.J. Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site Biosci.Rep., 35:-, 2015 Cited by PubMed Abstract: Epsilon class glutathione transferases (GSTs) have been shown to contribute significantly to insecticide resistance. We report a new Epsilon class protein crystal structure from Drosophila melanogaster for the glutathione transferase DmGSTE6. The structure reveals a novel Epsilon clasp motif that is conserved across hundreds of millions of years of evolution of the insect Diptera order. This histidine-serine motif lies in the subunit interface and appears to contribute to quaternary stability as well as directly connecting the two glutathiones in the active sites of this dimeric enzyme. PubMed: 26487708DOI: 10.1042/BSR20150183 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.72 Å) |
Structure validation
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