› 5ory

X-ray diffraction
1.99Å resolution

Crystal structure of Aurora-A kinase in complex with an allosterically binding fragment

Released:
DOI: 10.2210/pdb5ory/pdb
PDB entry 5ory coloured by chain, front view.
PDB entry 5ory coloured by chain, side view.
PDB entry 5ory coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Characterization of Three Druggable Hot-Spots in the Aurora-A/TPX2 Interaction Using Biochemical, Biophysical, and Fragment-Based Approaches.
McIntyre PJ, Collins PM, Vrzal L, Birchall K, Arnold LH, Mpamhanga C, Coombs PJ, Burgess SG, Richards MW, Winter A, Veverka V, Delft FV, Merritt A, Bayliss R
ACS Chem Biol 12 2906-2914 (2017)
PMID: 29045126

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: 265 amino acids
Theoretical weight: 30.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14965 (Residues: 127-391; Coverage: 66%)
Gene names: AIK, AIRK1, ARK1, AURA, AURKA, AYK1, BTAK, IAK1, STK15, STK6
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ADP 1 x ADP
Ligand MG 2 x MG
Ligand CL 3 x CL
Ligand AY4 1 x AY4
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P6122
Unit cell:
a: 82.14Å b: 82.14Å c: 176.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.204 0.265
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The multifaceted allosteric regulation of Aurora kinase A.
Levinson NM. (2018)
4 more