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4B65

A. fumigatus ornithine hydroxylase (SidA), reduced state bound to NADP(H)

Summary for 4B65
Entry DOI10.2210/pdb4b65/pdb
Related4B63 4B64 4B66 4B67 4B68 4B69
DescriptorL-ORNITHINE N5 MONOOXYGENASE, FLAVIN-ADENINE DINUCLEOTIDE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total)
Functional Keywordsoxidoreductase, siderophore, flavin
Biological sourceASPERGILLUS FUMIGATUS
Total number of polymer chains1
Total formula weight58955.09
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 citationFranceschini, 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: 22928747
DOI: 10.1021/BI301072W
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.32 Å)
Structure validation

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