2vou

X-ray diffraction
2.6Å resolution

Structure of 2,6-dihydroxypyridine-3-hydroxylase from Arthrobacter nicotinovorans

Released:

Function and Biology Details

Reaction catalysed:
2,6-dihydroxypyridine + NADH + O(2) = 2,3,6-trihydroxypyridine + NAD(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-188102 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,6-dihydroxypyridine 3-monooxygenase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 397 amino acids
Theoretical weight: 43.43 KDa
Source organism: Paenarthrobacter nicotinovorans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93NG3 (Residues: 1-397; Coverage: 100%)
Gene name: dhpH
Sequence domains: FAD binding domain
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 3 x FAD
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3221
Unit cell:
a: 185.96Å b: 185.96Å c: 104.76Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.185 0.222
Expression system: Escherichia coli BL21(DE3)