1OYC
OLD YELLOW ENZYME AT 2 ANGSTROMS RESOLUTION: OVERALL STRUCTURE, LIGAND BINDING AND COMPARISON WITH RELATED FLAVOPROTEINS
Summary for 1OYC
Entry DOI | 10.2210/pdb1oyc/pdb |
Descriptor | OLD YELLOW ENZYME, FLAVIN MONONUCLEOTIDE (3 entities in total) |
Functional Keywords | oxidoreductase(flavoprotein) |
Biological source | Saccharomyces pastorianus |
Total number of polymer chains | 1 |
Total formula weight | 45527.99 |
Authors | Fox, K.M.,Karplus, P.A. (deposition date: 1994-08-25, release date: 1994-11-30, Last modification date: 2024-02-14) |
Primary citation | Fox, K.M.,Karplus, P.A. Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins. Structure, 2:1089-1105, 1994 Cited by PubMed Abstract: Old yellow enzyme (OYE) was the first flavoenzyme purified, but its function is still unknown. Nevertheless, the NADPH oxidase activity, the flavin mononucleotide environment and the ligand-binding properties of OYE have been extensively studied by biochemical and spectroscopic approaches. Full interpretation of these data requires structural information. PubMed: 7881908DOI: 10.1016/S0969-2126(94)00111-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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