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5A8R

METHYL-COENZYME M REDUCTASE II FROM METHANOTHERMOBACTER MARBURGENSIS AT 2.15 A RESOLUTION

Summary for 5A8R
Entry DOI10.2210/pdb5a8r/pdb
Related5A8K 5A8W
DescriptorMETHYL-COENZYME M REDUCTASE II SUBUNIT ALPHA, METHYL-COENZYME M REDUCTASE II SUBUNIT GAMMA, METHYL-COENZYME M REDUCTASE II, SUBUNIT BETA, ... (8 entities in total)
Functional Keywordstransferase, post-translational modification, binding sites, catalysis, coenzymes, disulfides, hydrogen, hydrogen bonding, ligands, mesna, metalloporphyrins, methane, methanobacterium, models, molecular, nickel, oxidation-reduction, oxidoreductases, phosphothreonine, protein conformation, protein folding, protein structure
Biological sourceMETHANOTHERMOBACTER MARBURGENSIS
More
Total number of polymer chains12
Total formula weight559565.00
Authors
Wagner, T.,Ermler, U. (deposition date: 2015-07-16, release date: 2016-08-10, Last modification date: 2024-01-10)
Primary citationWagner, T.,Kahnt, J.,Ermler, U.,Shima, S.
Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation.
Angew.Chem.Int.Ed.Engl., 55:10630-, 2016
Cited by
PubMed: 27467699
DOI: 10.1002/ANIE.201603882
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

219515

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