5A8R
METHYL-COENZYME M REDUCTASE II FROM METHANOTHERMOBACTER MARBURGENSIS AT 2.15 A RESOLUTION
Summary for 5A8R
Entry DOI | 10.2210/pdb5a8r/pdb |
Related | 5A8K 5A8W |
Descriptor | METHYL-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 Keywords | transferase, 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 source | METHANOTHERMOBACTER MARBURGENSIS More |
Total number of polymer chains | 12 |
Total formula weight | 559565.00 |
Authors | Wagner, T.,Ermler, U. (deposition date: 2015-07-16, release date: 2016-08-10, Last modification date: 2024-01-10) |
Primary citation | Wagner, 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: 27467699DOI: 10.1002/ANIE.201603882 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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