PDBe 2xck

X-ray diffraction
2.3Å resolution

Crystal structure of PDK1 in complex with a pyrazoloquinazoline inhibitor

Released:
Source organism: Homo sapiens
Primary publication:
Structure-based optimization of potent PDK1 inhibitors.
Bioorg. Med. Chem. Lett. 20 4095-9 (2010)
PMID: 20621725

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-phosphoinositide-dependent protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 309 amino acids
Theoretical weight: 35.43 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O15530 (Residues: 51-359; Coverage: 56%)
Gene names: PDK1, PDPK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P3221
Unit cell:
a: 123.115Å b: 123.115Å c: 47.24Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.193 0.24
Expression system: Spodoptera frugiperda