Summary for 5UKA
| Entry DOI | 10.2210/pdb5uka/pdb |
| Descriptor | Alkyl hydroperoxide reductase subunit C, CHLORIDE ION, POTASSIUM ION, ... (5 entities in total) |
| Functional Keywords | peroxiredoxin, ff, prxi, conformation, oxidoreductase |
| Biological source | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Total number of polymer chains | 5 |
| Total formula weight | 103518.56 |
| Authors | Perkins, A.,Nelson, K.,Parsonage, D.,Poole, L.,Karplus, P.A. (deposition date: 2017-01-20, release date: 2018-01-24, Last modification date: 2023-10-04) |
| Primary citation | Nelson, K.J.,Perkins, A.,Van Swearingen, A.E.D.,Hartman, S.,Brereton, A.E.,Parsonage, D.,Salsbury Jr., F.R.,Karplus, P.A.,Poole, L.B. Experimentally Dissecting the Origins of Peroxiredoxin Catalysis. Antioxid.Redox Signal., 28:521-536, 2018 Cited by PubMed Abstract: Peroxiredoxins (Prxs) are ubiquitous cysteine-based peroxidases involved in oxidant defense and signal transduction. Despite much study, the precise roles of conserved residues remain poorly defined. In this study, we carried out extensive functional and structural characterization of 10 variants of such residues in a model decameric bacterial Prx. PubMed: 28375740DOI: 10.1089/ars.2016.6922 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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