2i5b

X-ray diffraction
2.8Å resolution

The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parralel emergence of enzyme activity during evolution

Released:

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-153905 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyridoxine kinase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 271 amino acids
Theoretical weight: 29.05 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P39610 (Residues: 1-271; Coverage: 100%)
Gene names: BSU38020, ipa-52r, pdxK, ywdB
Sequence domains: Phosphomethylpyrimidine kinase
Structure domains: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P41212
Unit cell:
a: 102.499Å b: 102.499Å c: 251.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.222 0.274
Expression system: Escherichia coli BL21