5N1Q

METHYL-COENZYME M REDUCTASE III FROM METHANOTHERMOCOCCUS THERMOLITHOTROPHICUS AT 1.9 A RESOLUTION

Summary for 5N1Q

Entry DOI	10.2210/pdb5n1q/pdb
Descriptor	METHYL-COENZYME M REDUCTASE III FROM METHANOTHERMOCOCCUS THERMOLITHOTROPHICUS SUBUNIT ALPHA, METHYL-COENZYME M REDUCTASE III FROM METHANOTHERMOCOCCUS THERMOLITHOTROPHICUS SUBUNIT BETA, METHYL-COENZYME M REDUCTASE III FROM METHANOTHERMOCOCCUS THERMOLITHOTROPHICUS SUBUNIT GAMMA, ... (10 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
Biological source	Methanothermococcus thermolithotrophicus DSM 2095 More
Total number of polymer chains	6
Total formula weight	280975.32
Authors	Wagner, T.,Wegner, C.E.,Ermler, U.,Shima, S. (deposition date: 2017-02-06, release date: 2017-06-14, Last modification date: 2024-05-01)
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 (1.9 Å)

Structure validation