1EGV
CRYSTAL STRUCTURE OF THE DIOL DEHYDRATASE-ADENINYLPENTYLCOBALAMIN COMPLEX FROM KLEBSELLA OXYTOCA UNDER THE ILLUMINATED CONDITION.
Summary for 1EGV
| Entry DOI | 10.2210/pdb1egv/pdb |
| Related | 1DIO 1EEX 1EGM |
| Descriptor | PROPANEDIOL DEHYDRATASE, POTASSIUM ION, CO-(ADENIN-9-YL-PENTYL)-COBALAMIN, ... (7 entities in total) |
| Functional Keywords | coenzyme b12, propanediol, potassium ion, tim barrel, lyase |
| Biological source | Klebsiella oxytoca More |
| Total number of polymer chains | 6 |
| Total formula weight | 210880.85 |
| Authors | Masuda, J.,Shibata, N.,Toraya, T.,Morimoto, Y.,Yasuoka, N. (deposition date: 2000-02-17, release date: 2001-02-21, Last modification date: 2024-03-13) |
| Primary citation | Masuda, J.,Shibata, N.,Morimoto, Y.,Toraya, T.,Yasuoka, N. How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex. Structure Fold.Des., 8:775-788, 2000 Cited by PubMed Abstract: Adenosylcobalamin (coenzyme B(12)) serves as a cofactor for enzymatic radical reactions. The adenosyl radical, a catalytic radical in these reactions, is formed by homolysis of the cobalt-carbon bond of the coenzyme, although the mechanism of cleavage of its organometallic bond remains unsolved. PubMed: 10903944DOI: 10.1016/S0969-2126(00)00164-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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