5A0Y
METHYL-COENZYME M REDUCTASE FROM METHANOTHERMOBACTER MARBURGENSIS AT 1.1 A RESOLUTION
Summary for 5A0Y
| Entry DOI | 10.2210/pdb5a0y/pdb |
| Descriptor | METHYL-COENZYME M REDUCTASE I SUBUNIT ALPHA, CHLORIDE ION, METHYL-COENZYME M REDUCTASE I SUBUNIT BETA, ... (11 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 | 6 |
| Total formula weight | 276758.20 |
| Authors | Wagner, T.,Ermler, U. (deposition date: 2015-04-24, release date: 2016-05-11, 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 (1.1 Å) |
Structure validation
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