› 4eoh

X-ray diffraction
2.1Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyridoxal kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 312 amino acids
Theoretical weight: 35.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • 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

4 bound ligands:
Ligand NA 2 x NA
Ligand TEP 2 x TEP
Ligand MPD 14 x MPD
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: I222
Unit cell:
a: 92.302Å b: 115.848Å c: 171.904Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.254
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Working group reports: evaluation of the evidence to support practice guidelines for nutritional care of preterm infants-the Pre-B Project.
Raiten et al. (2016)
1 more

2 mentions without citation

Identification of kinase inhibitor targets in the lung cancer microenvironment by chemical and phosphoproteomics.
Gridling et al. (2014)
1 more