1rfu

X-ray diffraction
2.8Å resolution

Crystal structure of pyridoxal kinase complexed with ADP and PLP

Released:
Source organism: Ovis aries
Primary publication:
Conformational changes in the reaction of pyridoxal kinase.
J Biol Chem 279 17459-65 (2004)
PMID: 14722069

Function and Biology Details

Reaction catalysed:
ATP + pyridoxal = ADP + pyridoxal 5'-phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160609 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyridoxal kinase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 312 amino acids
Theoretical weight: 34.86 KDa
Source organism: Ovis aries
UniProt:
  • Canonical: P82197 (Residues: 1-312; Coverage: 100%)
Gene names: PDXK, PKH
Sequence domains: Phosphomethylpyrimidine kinase
Structure domains: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43
Unit cell:
a: 109.088Å b: 109.088Å c: 284.272Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.229 0.281