1FF3
STRUCTURE OF THE PEPTIDE METHIONINE SULFOXIDE REDUCTASE FROM ESCHERICHIA COLI
Summary for 1FF3
| Entry DOI | 10.2210/pdb1ff3/pdb |
| Descriptor | PEPTIDE METHIONINE SULFOXIDE REDUCTASE, SULFATE ION (3 entities in total) |
| Functional Keywords | peptide methionine sulfoxide reductase, alpha beta roll, pmsr, msra, oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 3 |
| Total formula weight | 70310.56 |
| Authors | Tete-Favier, F.,Cobessi, D.,Boschi-Muller, S.,Azza, S.,Branlant, G.,Aubry, A. (deposition date: 2000-07-25, release date: 2000-12-06, Last modification date: 2011-07-13) |
| Primary citation | Tete-Favier, F.,Cobessi, D.,Boschi-Muller, S.,Azza, S.,Branlant, G.,Aubry, A. Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution. Structure Fold.Des., 8:1167-1178, 2000 Cited by PubMed Abstract: Peptide methionine sulphoxide reductases catalyze the reduction of oxidized methionine residues in proteins. They are implicated in the defense of organisms against oxidative stress and in the regulation of processes involving peptide methionine oxidation/reduction. These enzymes are found in numerous organisms, from bacteria to mammals and plants. Their primary structure shows no significant similarity to any other known protein. PubMed: 11080639DOI: 10.1016/S0969-2126(00)00526-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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