X-ray diffraction
2.5Å resolution

Crystal structure of D235A mutant of human pyridoxal kinase

Source organism: Homo sapiens
Entry authors: Safo MK, Gandhi AK, Musayev FN, Ghatge M, Di Salvo ML, Schirch V

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)
Entry contents:
1 distinct polypeptide molecule
Pyridoxal kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 312 amino acids
Theoretical weight: 35.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: O00764 (Residues: 1-312; Coverage: 100%)
Gene names: C21orf124, C21orf97, PDXK, PKH, PNK, PRED79
Sequence domains: Phosphomethylpyrimidine kinase
Structure domains: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I222
Unit cell:
a: 91.224Å b: 115.422Å c: 168.898Å
α: 90° β: 90° γ: 90°
R R work R free
0.214 0.212 0.262
Expression system: Escherichia coli