5j19

X-ray diffraction
2Å resolution

phospho-Pon binding-induced Plk1 dimerization

Released:
Primary publication:
Phospho-Pon Binding-Mediated Fine-Tuning of Plk1 Activity.
Structure 24 1110-9 (2016)
PMID: 27238966

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-132154 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase PLK1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 234 amino acids
Theoretical weight: 26.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P53350 (Residues: 367-594; Coverage: 38%)
Gene names: PLK, PLK1
Sequence domains: POLO box duplicated region
Structure domains: POLO box domain
Partner of Numb Chains: C, D
Molecule details ›
Chains: C, D
Length: 15 amino acids
Theoretical weight: 1.7 KDa
Source organism: Drosophila melanogaster
Expression system: Not provided
UniProt:
  • Canonical: O96561 (Residues: 52-66; Coverage: 2%)
Gene names: CG3346, pon

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2221
Unit cell:
a: 84.88Å b: 91.997Å c: 159.222Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.213 0.236
Expression systems:
  • Escherichia coli BL21
  • Not provided