› 4lkl

X-ray diffraction
1.58Å resolution

Crystal structure of Plk1 Polo-box domain in complex with PL-55

Released:
DOI: 10.2210/pdb4lkl/pdb
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PDB entry 4lkl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Exploring the binding nature of pyrrolidine pocket-dependent interactions in the polo-box domain of polo-like kinase 1.
Murugan RN, Ahn M, Lee WC, Kim HY, Song JH, Cheong C, Hwang E, Seo JH, Shin SY, Choi SH, Park JE, Bang JK
OpenAccess logo PLoS One 8 e80043 (2013)
PMID: 24223211

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-156771 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase PLK1 Chain: A
Molecule details ›
Chain: A
Length: 222 amino acids
Theoretical weight: 25.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53350 (Residues: 372-593; Coverage: 37%)
Gene names: PLK, PLK1
Sequence domains: POLO box duplicated region
Structure domains: POLO box domain
PL-55 Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 790 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand ADM 1 x ADM
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21
Unit cell:
a: 37.34Å b: 50.94Å c: 57Å
α: 90° β: 97.61° γ: 90°
R-values:
R R work R free
0.224 0.224 0.255
Expression systems:
  • Escherichia coli
  • Not provided

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Citations

5 review citations

Recent Advances and New Strategies in Targeting Plk1 for Anticancer Therapy.
Lee et al. (2015)
4 more

1 mention 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)

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