› 5ta6

X-ray diffraction
2.5Å resolution

Crystal structure of PLK1 in complex with a novel 5,6-dihydroimidazolo[1,5-f]pteridine inhibitor.

Released:
DOI: 10.2210/pdb5ta6/pdb
PDB entry 5ta6 coloured by chain, front view.
PDB entry 5ta6 coloured by chain, side view.
PDB entry 5ta6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-based design and SAR development of 5,6-dihydroimidazolo[1,5-f]pteridine derivatives as novel Polo-like kinase-1 inhibitors.
Kiryanov A, Natala S, Jones B, McBride C, Feher V, Lam B, Liu Y, Honda K, Uchiyama N, Kawamoto T, Hikichi Y, Zhang L, Hosfield D, Skene R, Zou H, Stafford J, Cao X, Ichikawa T
Bioorg Med Chem Lett 27 1311-1315 (2017)
PMID: 28169164

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156752 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase PLK1 Chain: A
Molecule details ›
Chain: A
Length: 358 amino acids
Theoretical weight: 40.58 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: P53350 (Residues: 13-345; Coverage: 55%)
Gene names: PLK, PLK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 79D 1 x 79D
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P3221
Unit cell:
a: 66.303Å b: 66.303Å c: 153.115Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.179 0.26
Expression system: unidentified baculovirus

Quick links

Citations

1 review citation

Therapeutic potential of pteridine derivatives: A comprehensive review.
Carmona-Martínez et al. (2019)
2 other articles

2 mentions without citation

CRISPRO: identification of functional protein coding sequences based on genome editing dense mutagenesis.
Schoonenberg et al. (2018)
1 more