› 6x0i

X-ray diffraction
1.95Å resolution

Structure of oxidized SidA ornithine hydroxylase with the FAD "in" and complexed with NADP

Released:
DOI: 10.2210/pdb6x0i/pdb
PDB 6x0i coloured by chain and viewed from the front.
PDB 6x0i coloured by chain and viewed from the side.
PDB 6x0i coloured by chain and viewed from the top.
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:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ornithine N(5)-monooxygenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 501 amino acids
Theoretical weight: 56.96 KDa
Source organism: Aspergillus fumigatus Af293
Expression system: Escherichia coli
UniProt:
  • Canonical: E9QYP0 (Residues: 1-501; Coverage: 100%)
Gene names: Afu2g07680, sidA
Sequence domains: L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD

Cofactor: Ligand NAP 4 x NAP
2 bound ligands:
Ligand ACT 4 x ACT
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 80.507Å b: 154.868Å c: 90.483Å
α: 90° β: 109.25° γ: 90°
R-values:
R R work R free
0.17 0.168 0.211
Expression system: Escherichia coli

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