› 4hy2

X-ray diffraction
2Å resolution

Crystal structure of Plk1 Polo-box domain in complex with PL-42

Released:
DOI: 10.2210/pdb4hy2/pdb
PDB entry 4hy2 coloured by chain, front view.
PDB entry 4hy2 coloured by chain, side view.
PDB entry 4hy2 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-547114 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase PLK1 Chain: A
Molecule details ›
Chain: A
Length: 225 amino acids
Theoretical weight: 26.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53350 (Residues: 371-595; Coverage: 37%)
Gene names: PLK, PLK1
Sequence domains: POLO box duplicated region
Structure domains: POLO box domain
PL-42 Chain: D
Molecule details ›
Chain: D
Length: 7 amino acids
Theoretical weight: 944 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-1A
Spacegroup: P21
Unit cell:
a: 35.425Å b: 50.262Å c: 57.456Å
α: 90° β: 101.515° γ: 90°
R-values:
R R work R free
0.199 0.199 0.246
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

2 mentions without citation

Exploring the binding nature of pyrrolidine pocket-dependent interactions in the polo-box domain of polo-like kinase 1.
Murugan et al. (2013)
1 more