X-ray diffraction
2.28Å resolution

Function and Biology Details

Reaction catalysed:
1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 H(2)O
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Pyridoxine 5'-phosphate synthase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 278 amino acids
Theoretical weight: 29.84 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
  • Canonical: Q3JQ80 (Residues: 1-257; Coverage: 100%)
Gene names: BURPS1710b_2892, pdxJ
Sequence domains: Pyridoxal phosphate biosynthesis protein PdxJ
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P1
Unit cell:
a: 90.09Å b: 91.864Å c: 90.024Å
α: 118.48° β: 116.81° γ: 93.5°
R R work R free
0.189 0.186 0.245
Expression system: Escherichia coli