4tm0

X-ray diffraction
2.74Å resolution

Kutzneria sp. 744 ornithine N-hydroxylase, KtzI-FADred-ox-NADP+-L-orn

Released:
Source organism: Kutzneria sp. 744
Entry authors: Setser JW, Drennan CL

Function and Biology Details

Reaction catalysed:
L-lysine + NADPH + O(2) = N(6)-hydroxy-L-lysine + NADP(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lysine N6-monooxygenase MbtG Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 443 amino acids
Theoretical weight: 49.43 KDa
Source organism: Kutzneria sp. 744
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A8CF85 (Residues: 3-424; Coverage: 100%)
Gene names: KUTG_08917, ktzI
Sequence domains: L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 85.029Å b: 156.401Å c: 164.496Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.216
Expression system: Escherichia coli BL21