1nrg

X-ray diffraction
1.95Å resolution

Structure and Properties of Recombinant Human Pyridoxine-5'-Phosphate Oxidase

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction catalysed:
Pyridoxamine 5'-phosphate + H(2)O + O(2) = pyridoxal 5'-phosphate + NH(3) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyridoxine-5'-phosphate oxidase Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 30.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NVS9 (Residues: 1-261; Coverage: 100%)
Gene name: PNPO
Sequence domains:
Structure domains: Electron Transport, Fmn-binding Protein; Chain A

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 82.747Å b: 82.747Å c: 59.327Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.192 0.253
Expression system: Escherichia coli