5L71
Crystal structure of mouse phospholipid hydroperoxide glutathione peroxidase 4 (GPx4)
Summary for 5L71
| Entry DOI | 10.2210/pdb5l71/pdb |
| Descriptor | Phospholipid hydroperoxide glutathione peroxidase, mitochondrial, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | phospholipid hydroperoxide glutathione peroxidase 4 (gpx4), selenocysteine, oxidoreductase |
| Biological source | Mus musculus (Mouse) |
| Cellular location | Mitochondrion : O70325 |
| Total number of polymer chains | 1 |
| Total formula weight | 19745.79 |
| Authors | Janowski, R.,Scanu, S.,Madl, T.,Niessing, D. (deposition date: 2016-06-01, release date: 2016-10-19, Last modification date: 2024-01-10) |
| Primary citation | Janowski, R.,Scanu, S.,Niessing, D.,Madl, T. Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4. Acta Crystallogr.,Sect.F, 72:743-749, 2016 Cited by PubMed Abstract: The mammalian glutathione peroxidase (GPx) family is a key component of the cellular antioxidative defence system. Within this family, GPx4 has unique features as it accepts a large class of hydroperoxy lipid substrates and has a plethora of biological functions, including sperm maturation, regulation of apoptosis and cerebral embryogenesis. In this paper, the structure of the cytoplasmic isoform of mouse phospholipid hydroperoxide glutathione peroxidase (O70325-2 GPx4) with selenocysteine 46 mutated to cysteine is reported solved at 1.8 Å resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented. PubMed: 27710939DOI: 10.1107/S2053230X16013686 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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