› 4d7e

X-ray diffraction
2.4Å resolution

An unprecedented NADPH domain conformation in Lysine Monooxygenase NbtG from Nocardia farcinica

Released:
DOI: 10.2210/pdb4d7e/pdb
PDB entry 4d7e coloured by chain, front view.
PDB entry 4d7e coloured by chain, side view.
PDB entry 4d7e coloured by chain, top view.
Source organism: Nocardia farcinica IFM 10152
Primary publication:
An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation.
Binda C, Robinson RM, Martin Del Campo JS, Keul ND, Rodriguez PJ, Robinson HH, Mattevi A, Sobrado P
J Biol Chem 290 12676-88 (2015)
PMID: 25802330

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178547 (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: 429 amino acids
Theoretical weight: 46.6 KDa
Source organism: Nocardia farcinica IFM 10152
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5Z1T5 (Residues: 1-429; Coverage: 100%)
Gene names: NFA_7610, nbtG
Sequence domains: L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P21
Unit cell:
a: 80.64Å b: 121.92Å c: 91.86Å
α: 90° β: 97.72° γ: 90°
R-values:
R R work R free
0.211 0.208 0.281
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Regulated methionine oxidation by monooxygenases.
Manta et al. (2017)
3 more

1 mention without citation

An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation.
Binda et al. (2015)