› 5xvu

X-ray diffraction
3Å resolution

Crystal structure of the protein kinase CK2 catalytic domain from Plasmodium falciparum bound to ATP

Released:
DOI: 10.2210/pdb5xvu/pdb
PDB entry 5xvu coloured by chain, front view.
PDB entry 5xvu coloured by chain, side view.
PDB entry 5xvu coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
The protein kinase CK2 catalytic domain from Plasmodium falciparum: crystal structure, tyrosine kinase activity and inhibition.
Ruiz-Carrillo D, Lin J, El Sahili A, Wei M, Sze SK, Cheung PCF, Doerig C, Lescar J
OpenAccess logo Sci Rep 8 7365 (2018)
PMID: 29743645

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-568827 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein kinase domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 332 amino acids
Theoretical weight: 39.7 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IIR9 (Residues: 12-335; Coverage: 97%)
Gene name: PF3D7_1108400
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand SO4 5 x SO4
Ligand CL 3 x CL
Ligand ATP 3 x ATP
Ligand EDO 4 x EDO
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 88.41Å b: 123.55Å c: 125.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.216
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Plasmodial Kinase Inhibitors Targeting Malaria: Recent Developments.
Mustière et al. (2020)
3 more

5 mentions without citation

Plasmodium Kinases as Potential Drug Targets for Malaria: Challenges and Opportunities.
Arendse et al. (2021)
4 more