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: 28559298 DOI: 10.1128/JB.00197-17 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation