› 2ogq

X-ray diffraction
1.95Å resolution

Molecular and structural basis of Plk1 substrate recognition: Implications in centrosomal localization

Released:
DOI: 10.2210/pdb2ogq/pdb
PDB entry 2ogq coloured by chain, front view.
PDB entry 2ogq coloured by chain, side view.
PDB entry 2ogq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization.
García-Alvarez B, de Cárcer G, Ibañez S, Bragado-Nilsson E, Montoya G
Proc Natl Acad Sci U S A 104 3107-12 (2007)
PMID: 17307877

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156752 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase PLK1 Chain: A
Molecule details ›
Chain: A
Length: 239 amino acids
Theoretical weight: 27.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53350 (Residues: 365-603; Coverage: 40%)
Gene names: PLK, PLK1
Sequence domains: POLO box duplicated region
Structure domains: POLO box domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21212
Unit cell:
a: 77.051Å b: 99.017Å c: 33.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.159 0.221
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Cell cycle kinases as therapeutic targets for cancer.
Lapenna et al. (2009)
18 more

6 mentions without citation

PLK-1 Targeted Inhibitors and Their Potential against Tumorigenesis.
Kumar et al. (2015)
5 more