5N28
METHYL-COENZYME M REDUCTASE III FROM METHANOTORRIS FORMICICUS MONOCLINIC FORM
Summary for 5N28
Entry DOI | 10.2210/pdb5n28/pdb |
Descriptor | Methyl-coenzyme M reductase subunit alpha, Methyl-coenzyme M reductase, beta subunit, Methyl-coenzyme M reductase, gamma subunit, ... (8 entities in total) |
Functional Keywords | transferase, post-translational modification, binding sites, catalysis, coenzymes, disulfides, hydrogen, hydrogen bonding, ligands, mesna, metalloporphyrins, methane, methanococcales, nickel, oxidation-reduction, oxidoreductases, phosphothreonine, protein conformation, protein folding, protein structure, thermophile, autotroph, hydroxy-tryptophane |
Biological source | Methanotorris formicicus Mc-S-70 More |
Total number of polymer chains | 6 |
Total formula weight | 280817.35 |
Authors | Wagner, T.,Wegner, C.E.,Ermler, U.,Shima, S. (deposition date: 2017-02-07, release date: 2017-06-14, Last modification date: 2024-01-17) |
Primary citation | Wagner, T.,Wegner, C.E.,Kahnt, J.,Ermler, U.,Shima, S. Phylogenetic and Structural Comparisons of the Three Types of Methyl Coenzyme M Reductase from Methanococcales and Methanobacteriales. J.Bacteriol., 199:-, 2017 Cited by PubMed: 28559298DOI: 10.1128/JB.00197-17 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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