1SIJ
Crystal structure of the Aldehyde Dehydrogenase (a.k.a. AOR or MOP) of Desulfovibrio gigas covalently bound to [AsO3]-
Summary for 1SIJ
Entry DOI | 10.2210/pdb1sij/pdb |
Related | 1HLR |
Descriptor | Aldehyde oxidoreductase, CHLORIDE ION, MAGNESIUM ION, ... (7 entities in total) |
Functional Keywords | aldehyde oxidoreductase; xanthine oxidase family; arsenite inhibition, oxidoreductase |
Biological source | Desulfovibrio gigas |
Total number of polymer chains | 1 |
Total formula weight | 98614.51 |
Authors | Boer, D.R.,Thapper, A.,Brondino, C.D.,Romao, M.J.,Moura, J.J.G. (deposition date: 2004-03-01, release date: 2004-07-27, Last modification date: 2023-08-23) |
Primary citation | Boer, D.R.,Thapper, A.,Brondino, C.D.,Romao, M.J.,Moura, J.J.G. X-ray Crystal Structure and EPR Spectra of "Arsenite-Inhibited" Desulfovibriogigas Aldehyde Dehydrogenase: A Member of the Xanthine Oxidase Family J.Am.Chem.Soc., 126:8614-8615, 2004 Cited by PubMed Abstract: X-ray crystallography has been used to determine the structure of arsenite-inhibited aldehyde dehydrogenase from Desulfovibrio gigas, a member of the xanthine oxidase family of mononuclear molybdenum enzymes. The structure shows an AsO3 moiety bound to the molybdenum atom of the active site through one of the oxygen atoms. A reduced sample of arsenite-inhibited aldehyde dehydrogenase has a Mo(V) signal that shows anisotropic hyperfine and quadrupole coupling to one arsenic atom. This signal has a strong resemblance with a previously reported signal for arsenite-inhibited xanthine oxidase. PubMed: 15250689DOI: 10.1021/ja0490222 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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