› 1ixp

X-ray diffraction
2.3Å resolution

Enzyme-phosphate Complex of Pyridoxine 5'-Phosphate synthase

Released:
DOI: 10.2210/pdb1ixp/pdb
PDB entry 1ixp coloured by chain, front view.
PDB entry 1ixp coloured by chain, side view.
PDB entry 1ixp coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Enzyme-ligand complexes of pyridoxine 5'-phosphate synthase: implications for substrate binding and catalysis.
Garrido-Franco M, Laber B, Huber R, Clausen T
J Mol Biol 321 601-12 (2002)
PMID: 12206776

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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo octamer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141563 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyridoxine 5'-phosphate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 242 amino acids
Theoretical weight: 26.29 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A794 (Residues: 2-243; Coverage: 100%)
Gene names: JW2548, b2564, pdxJ
Sequence domains: Pyridoxal phosphate biosynthesis protein PdxJ
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand PO4 8 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 132Å b: 154.8Å c: 130.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.21 0.266
Expression system: Escherichia coli

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Citations

2 review citations

Cofactor biosynthesis: an organic chemist's treasure trove.
Begley TP. (2006)
1 more