PDBe 4da5

X-ray diffraction
2.4Å resolution

Choline Kinase alpha acts through a double-displacement kinetic mechanism involving enzyme isomerisation, as determined through enzyme and inhibitor kinetics and structural biology

Released:
Source organism: Homo sapiens
Primary publication:
Kinetic and mechanistic characterisation of Choline Kinase-α.
Biochim. Biophys. Acta 1834 1107-16 (2013)
PMID: 23416529

Function and Biology Details

Reactions catalysed:
ATP + choline = ADP + phosphocholine. 
ATP + ethanolamine = ADP + O-phosphoethanolamine. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Choline kinase alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 457 amino acids
Theoretical weight: 52.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35790 (Residues: 1-457; Coverage: 100%)
Gene names: CHK, CHKA, CKI
Sequence domains: Choline/ethanolamine kinase
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 55.84Å b: 121.69Å c: 131.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.259
Expression system: Escherichia coli BL21(DE3)