› 1v0p

X-ray diffraction
2Å resolution

Structure of P. falciparum PfPK5-Purvalanol B ligand complex

Released:
DOI: 10.2210/pdb1v0p/pdb
PDB entry 1v0p coloured by chain, front view.
PDB entry 1v0p coloured by chain, side view.
PDB entry 1v0p coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Structures of P. falciparum PfPK5 test the CDK regulation paradigm and suggest mechanisms of small molecule inhibition.
Holton S, Merckx A, Burgess D, Doerig C, Noble M, Endicott J
Structure 11 1329-37 (2003)
PMID: 14604523

Function and Biology Details

Reactions catalysed: 
ATP + a protein = ADP + a phosphoprotein
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170500 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclin-dependent kinase 2 homolog Chains: A, B
Molecule details ›
Chains: A, B
Length: 288 amino acids
Theoretical weight: 33.06 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07785 (Residues: 1-288; Coverage: 100%)
Gene names: CRK2, PK5
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 222.64Å b: 44.361Å c: 63.762Å
α: 90° β: 103.19° γ: 90°
R-values:
R R work R free
0.198 0.194 0.265
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote.
Ward et al. (2004)
16 more

16 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
15 more