› 4b68

X-ray diffraction
2.29Å resolution

A. fumigatus ornithine hydroxylase (SidA), re-oxidised state bound to NADP and Arg

Released:
DOI: 10.2210/pdb4b68/pdb
PDB entry 4b68 coloured by chain, front view.
PDB entry 4b68 coloured by chain, side view.
PDB entry 4b68 coloured by chain, top view.
Source organism: Aspergillus fumigatus
Primary publication:
Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases.
Franceschini S, Fedkenheuer M, Vogelaar NJ, Robinson HH, Sobrado P, Mattevi A
Biochemistry 51 7043-5 (2012)
PMID: 22928747

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-514170 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ornithine N(5)-monooxygenase Chain: A
Molecule details ›
Chain: A
Length: 501 amino acids
Theoretical weight: 56.96 KDa
Source organism: Aspergillus fumigatus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: E9QYP0 (Residues: 1-501; Coverage: 100%)
Gene names: Afu2g07680, sidA
Sequence domains: L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP

Cofactor: Ligand FAD 1 x FAD
3 bound ligands:
Ligand ARG 1 x ARG
Ligand SO4 1 x SO4
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: I222
Unit cell:
a: 77.53Å b: 84.73Å c: 145.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.217 0.269
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

Fungal siderophore metabolism with a focus on Aspergillus fumigatus.
Haas H. (2014)
8 more