› 3zm9

X-ray diffraction
1.9Å resolution

The mechanism of allosteric coupling in choline kinase a1 revealed by a rationally designed inhibitor

Released:
DOI: 10.2210/pdb3zm9/pdb
PDB entry 3zm9 coloured by chain, front view.
PDB entry 3zm9 coloured by chain, side view.
PDB entry 3zm9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The mechanism of allosteric coupling in choline kinase α1 revealed by the action of a rationally designed inhibitor.
Sahún-Roncero M, Rubio-Ruiz B, Saladino G, Conejo-García A, Espinosa A, Velázquez-Campoy A, Gervasio FL, Entrena A, Hurtado-Guerrero R
Angew Chem Int Ed Engl 52 4582-6 (2013)
PMID: 23441033

Function and Biology Details

Reactions catalysed: 
ATP + choline = ADP + phosphocholine
ATP + ethanolamine = ADP + O-phosphoethanolamine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153022 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Choline kinase alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 44.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35790 (Residues: 75-457; Coverage: 84%)
Gene names: CHK, CHKA, CKI
Sequence domains: Choline/ethanolamine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand QMQ 2 x QMQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 55.746Å b: 121.214Å c: 131.861Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.201 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Harnessing allostery: a novel approach to drug discovery.
Lu et al. (2014)
1 more

2 mentions without citation

Design, synthesis, crystallization and biological evaluation of new symmetrical biscationic compounds as selective inhibitors of human Choline Kinase α1 (ChoKα1).
Schiaffino-Ortega et al. (2016)
1 more