› 1g77

X-ray diffraction
2.1Å resolution

X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5`-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION

Released:
DOI: 10.2210/pdb1g77/pdb
PDB entry 1g77 coloured by chain, front view.
PDB entry 1g77 coloured by chain, side view.
PDB entry 1g77 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with pyridoxal 5'-phosphate at 2.0 A resolution.
Safo MK, Musayev FN, di Salvo ML, Schirch V
J Mol Biol 310 817-26 (2001)
PMID: 11453690

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142729 (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:
Ligand PO4 2 x PO4
Ligand PLP 1 x PLP
1 modified residue:
Ligand MSE 5 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 63.44Å b: 63.44Å c: 124.64Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.209 0.236
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The human flavoproteome.
Lienhart et al. (2013)
2 more

3 mentions without citation

Rv2607 from Mycobacterium tuberculosis is a pyridoxine 5'-phosphate oxidase with unusual substrate specificity.
Mashalidis et al. (2011)
2 more