› 2xne

X-ray diffraction
2.8Å resolution

Structure of Aurora-A bound to an imidazopyrazine inhibitor

Released:
DOI: 10.2210/pdb2xne/pdb
PDB entry 2xne coloured by chain, front view.
PDB entry 2xne coloured by chain, side view.
PDB entry 2xne coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-based design of imidazo[1,2-a]pyrazine derivatives as selective inhibitors of Aurora-A kinase in cells.
Bouloc N, Large JM, Kosmopoulou M, Sun C, Faisal A, Matteucci M, Reynisson J, Brown N, Atrash B, Blagg J, McDonald E, Linardopoulos S, Bayliss R, Bavetsias V
Bioorg Med Chem Lett 20 5988-93 (2010)
PMID: 20833547

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-127232 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aurora kinase A Chain: A
Molecule details ›
Chain: A
Length: 272 amino acids
Theoretical weight: 31.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14965 (Residues: 122-392; Coverage: 67%)
Gene names: AIK, AIRK1, ARK1, AURA, AURKA, AYK1, BTAK, IAK1, STK15, STK6
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ASH 1 x ASH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P6122
Unit cell:
a: 82.923Å b: 82.923Å c: 167.092Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.24 0.238 0.281
Expression system: Escherichia coli

Quick links

Citations

5 review citations

On the molecular mechanisms of mitotic kinase activation.
Bayliss et al. (2012)
4 more