› 4hab

X-ray diffraction
2.65Å resolution

Crystal structure of Plk1 Polo-box domain in complex with PL-49

Released:
DOI: 10.2210/pdb4hab/pdb
PDB entry 4hab coloured by chain, front view.
PDB entry 4hab coloured by chain, side view.
PDB entry 4hab coloured by chain, top view.
Source organisms:
Primary publication:
Development of cyclic peptomer inhibitors targeting the polo-box domain of polo-like kinase 1.
Murugan RN, Park JE, Lim D, Ahn M, Cheong C, Kwon T, Nam KY, Choi SH, Kim BY, Yoon DY, Yaffe MB, Yu DY, Lee KS, Bang JK
Bioorg Med Chem 21 2623-34 (2013)
PMID: 23498919

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156769 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase PLK1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 223 amino acids
Theoretical weight: 25.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53350 (Residues: 371-593; Coverage: 37%)
Gene names: PLK, PLK1
Sequence domains: POLO box duplicated region
Structure domains: POLO box domain
PL-49 Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 7 amino acids
Theoretical weight: 860 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand CXS 5 x CXS
Ligand PO4 1 x PO4
2 modified residues:
Ligand 11Q 3 x 11Q
Ligand TPO 3 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-1A
Spacegroup: P43212
Unit cell:
a: 95.043Å b: 95.043Å c: 240.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.26 0.26 0.259
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

7 review citations

Modulating protein-protein interactions: the potential of peptides.
Nevola et al. (2015)
6 more

3 mentions without citation

Calmodulin: A Multitasking Protein in Kv7.2 Potassium Channel Functions.
Alaimo et al. (2018)
2 more