4B67
A. fumigatus ornithine hydroxylase (SidA), re-oxidised state bound to NADP and ornithine
Summary for 4B67
| Entry DOI | 10.2210/pdb4b67/pdb |
| Related | 4B63 4B64 4B65 4B66 4B68 4B69 |
| Descriptor | L-ORNITHINE N5 MONOOXYGENASE, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (7 entities in total) |
| Functional Keywords | oxidoreductase, siderophore |
| Biological source | ASPERGILLUS FUMIGATUS |
| Total number of polymer chains | 1 |
| Total formula weight | 59169.34 |
| Authors | Franceschini, S.,Fedkenheuer, M.,Vogelaar, N.J.,Robinson, H.H.,Sobrado, P.,Mattevi, A. (deposition date: 2012-08-09, release date: 2012-10-03, Last modification date: 2023-12-20) |
| Primary citation | Franceschini, S.,Fedkenheuer, M.,Vogelaar, N.J.,Robinson, H.H.,Sobrado, P.,Mattevi, A. Structural Insight Into the Mechanism of Oxygen Activation and Substrate Selectivity of Flavin-Dependent N-Hydroxylating Monooxygenases. Biochemistry, 51:7043-, 2012 Cited by PubMed Abstract: SidA from the human pathogen Aspergillus fumigatus catalyzes the generation of N(5)-hydroxyornithine in the biosynthesis of siderophores, a reaction essential for virulence. The crystal structures of SidA in complex with ornithine and lysine reveal the geometry of the interactions among flavin, NADP(+), and the substrate amine group that underlie the hydroxylation reaction. The structural elucidation of the enzyme in complex with arginine provides insight into the role of electrostatics and hydrogen bonding in the mechanism of oxygen activation in this family of enzymes. PubMed: 22928747DOI: 10.1021/BI301072W PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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