1jnw

X-ray diffraction
2.07Å resolution

Active Site Structure of E. coli pyridoxine 5'-phosphate Oxidase

Released:

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/pyridoxamine 5'-phosphate oxidase Chain: A
Molecule details ›
Chain: A
Length: 218 amino acids
Theoretical weight: 25.82 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AFI7 (Residues: 1-218; Coverage: 100%)
Gene names: JW1630, b1638, pdxH
Sequence domains:
Structure domains: Electron Transport, Fmn-binding Protein; Chain A

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 83.358Å b: 52.238Å c: 53.913Å
α: 90° β: 101.45° γ: 90°
R-values:
R R work R free
0.182 0.178 0.231
Expression system: Escherichia coli