› 5nn2

X-ray diffraction
1.81Å resolution

The structure of the polo-box domain (PBD) of Plk1 in complex with Z228588490

Released:
DOI: 10.2210/pdb5nn2/pdb
PDB entry 5nn2 coloured by chain, front view.
PDB entry 5nn2 coloured by chain, side view.
PDB entry 5nn2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A cryptic hydrophobic pocket in the polo-box domain of the polo-like kinase PLK1 regulates substrate recognition and mitotic chromosome segregation.
Sharma P, Mahen R, Rossmann M, Stokes JE, Hardwick B, Huggins DJ, Emery A, Kunciw DL, Hyvönen M, Spring DR, McKenzie GJ, Venkitaraman AR
Sci Rep 9 15930 (2019)
PMID: 31685831

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 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: 232 amino acids
Theoretical weight: 26.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53350 (Residues: 371-594; Coverage: 37%)
Gene names: PLK, PLK1
Sequence domains: POLO box duplicated region
Structure domains: POLO box domain

Ligands and Environments

1 bound ligand:
Ligand Z24 1 x Z24
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 33.36Å b: 93.38Å c: 35.9Å
α: 90° β: 100.72° γ: 90°
R-values:
R R work R free
0.189 0.187 0.219
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs.
Kliche et al. (2022)
1 more

2 mentions without citation

Discovery of a Potent PLK1-PBD Small-Molecule Inhibitor as an Anticancer Drug Candidate through Structure-Based Design.
Zhou et al. (2019)
1 more