› 6x0k

X-ray diffraction
2.23Å resolution

Structure of dithionite-reduced SidA ornithine hydroxylase with the FAD "in" and complexed with L-ornithine

Released:
DOI: 10.2210/pdb6x0k/pdb
PDB entry 6x0k coloured by chain, front view.
PDB entry 6x0k coloured by chain, side view.
PDB entry 6x0k coloured by chain, top view.
Source organism: Aspergillus fumigatus Af293
Primary publication:
Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics.
Campbell AC, Stiers KM, Martin Del Campo JS, Mehra-Chaudhary R, Sobrado P, Tanner JJ
J Biol Chem 295 13239-13249 (2020)
PMID: 32723870

Function and Biology Details

Reaction catalysed: 
L-ornithine + NAD(P)H + O(2) = N(5)-hydroxy-L-ornithine + NAD(P)(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123229 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ornithine N(5)-monooxygenase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 494 amino acids
Theoretical weight: 55.98 KDa
Source organism: Aspergillus fumigatus Af293
Expression system: Escherichia coli
UniProt:
  • Canonical: E9QYP0 (Residues: 29-501; Coverage: 94%)
Gene names: Afu2g07680, sidA
Sequence domains: L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase

Ligands and Environments


Cofactor: Ligand FDA 8 x FDA
1 bound ligand:
Ligand ORN 6 x ORN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 105.902Å b: 155.044Å c: 146.846Å
α: 90° β: 91.01° γ: 90°
R-values:
R R work R free
0.233 0.231 0.281
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Unifying and versatile features of flavin-dependent monooxygenases: Diverse catalysis by a common C4a-(hydro)peroxyflavin.
Phintha et al. (2023)
1 other article

1 mention without citation

Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics.
Campbell et al. (2020)