› 7jvl

X-ray diffraction
2.1Å resolution

Structure of the M101A variant of the SidA ornithine hydroxylase complexed with NADP and the FAD in the "out" conformation

Released:
DOI: 10.2210/pdb7jvl/pdb
PDB entry 7jvl coloured by chain, front view.
PDB entry 7jvl coloured by chain, side view.
PDB entry 7jvl coloured by chain, top view.
Source organism: Aspergillus fumigatus Af293
Primary publication:
Structural Determinants of Flavin Dynamics in a Class B Monooxygenase.
Campbell AC, Robinson R, Mena-Aguilar D, Sobrado P, Tanner JJ
Biochemistry 59 4609-4616 (2020)
PMID: 33226785

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
Molecule details ›
Chains: A, B, C, D
Length: 501 amino acids
Theoretical weight: 56.9 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 8 x ACT
Ligand CA 2 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: 80.229Å b: 153.811Å c: 89.87Å
α: 90° β: 109.28° γ: 90°
R-values:
R R work R free
0.205 0.204 0.241
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Ancestral reconstruction of mammalian FMO1 enables structural determination, revealing unique features that explain its catalytic properties.
Bailleul et al. (2021)
1 more