8CP2
Structure of Aspartate-N-hydroxylase (FzmM)from Streptomyces sp. V2: complex with NADPH and L-aspartate
Summary for 8CP2
Entry DOI | 10.2210/pdb8cp2/pdb |
Descriptor | FAD-binding protein, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (8 entities in total) |
Functional Keywords | monooxygenase, flavin, aspartate, oxidoreductase |
Biological source | Streptomyces sp. V2 |
Total number of polymer chains | 2 |
Total formula weight | 135965.64 |
Authors | Rotilio, L.,Mattevi, A. (deposition date: 2023-03-01, release date: 2023-07-12, Last modification date: 2024-06-19) |
Primary citation | Rotilio, L.,Boverio, A.,Nguyen, Q.T.,Mannucci, B.,Fraaije, M.W.,Mattevi, A. A biosynthetic aspartate N-hydroxylase performs successive oxidations by holding intermediates at a site away from the catalytic center. J.Biol.Chem., 299:104904-104904, 2023 Cited by PubMed: 37302552DOI: 10.1016/j.jbc.2023.104904 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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