4e9c

X-ray diffraction
1.7Å resolution

The structure of the polo-box domain (PBD) of polo-like kinase 1 (Plk1) in complex with LDPPLHSpTA phosphopeptide

Released:
Source organism: Homo sapiens
Primary publication:
High-throughput interrogation of ligand binding mode using a fluorescence-based assay.
Angew Chem Int Ed Engl 51 7680-3 (2012)
PMID: 22730171

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-156767 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
LDPPLHSpTA phosphopeptide Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.06 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 35.634Å b: 89.784Å c: 37.108Å
α: 90° β: 109.28° γ: 90°
R-values:
R R work R free
0.194 0.192 0.232
Expression systems:
  • Escherichia coli
  • Not provided