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5N2A

METHYL-COENZYME M REDUCTASE III FROM METHANOTORRIS FORMICICUS TRIGONAL FORM

Summary for 5N2A
Entry DOI10.2210/pdb5n2a/pdb
DescriptorMethyl-coenzyme M reductase subunit alpha, Methyl-coenzyme M reductase, beta subunit, Methyl-coenzyme M reductase, gamma subunit, ... (8 entities in total)
Functional Keywordstransferase, 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 sourceMethanotorris formicicus Mc-S-70
More
Total number of polymer chains3
Total formula weight140508.13
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 citationWagner, 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

221051

건을2024-06-12부터공개중

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