PDBe 2vrx

X-ray diffraction
1.86Å resolution

Structure of Aurora B kinase in complex with ZM447439

Released:
Source organism: Xenopus laevis
Primary publication:
Molecular basis of drug resistance in aurora kinases.
Chem. Biol. 15 552-62 (2008)
PMID: 18559266

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Inner centromere protein A Chains: C, D
Molecule details ›
Chains: C, D
Length: 43 amino acids
Theoretical weight: 4.98 KDa
Source organism: Xenopus laevis
UniProt:
  • Canonical: O13024 (Residues: 798-840; Coverage: 5%)
Gene name: incenp-a
Aurora kinase B-A Chains: A, B
Molecule details ›
Chains: A, B
Length: 285 amino acids
Theoretical weight: 33.65 KDa
Source organism: Xenopus laevis
UniProt:
  • Canonical: Q6DE08 (Residues: 77-361; Coverage: 79%)
Gene names: airk2-a, aurkb-a
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 45.735Å b: 67.004Å c: 116.583Å
α: 90° β: 96.93° γ: 90°
R-values:
R R work R free
0.191 0.188 0.243