Structure analysis

Crystal structure of the mouse Aurora-A catalytic domain (Asn186->Gly, Lys240->Arg, Met302->Leu) in complex with Compound 290.

X-ray diffraction
1.8Å resolution
Source organism: Mus musculus
Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo dimer
Accessible surface area: 23941.48 Å2
Buried surface area: 4463.8 Å2
Dissociation area: 2,231.9 Å2
Dissociation energy (ΔGdiss): 22.72 kcal/mol
Dissociation entropy (TΔSdiss): 13.64 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-161309
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 14202.64 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-161308

Macromolecules

Chain: A
Length: 272 amino acids
Theoretical weight: 31.55 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P97477 (Residues: 116-381; Coverage: 67%)
Gene names: Aik, Airk1, Ark1, Aura, Aurka, Ayk1, Btak, Iak1, Stk15, Stk6
Pfam: Protein kinase domain
InterPro:
CATH:

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