› 5obr

X-ray diffraction
2.62Å resolution

Aurora A kinase in complex with 2-(3-chloro-5-fluorophenyl)quinoline-4-carboxylic acid and JNJ-7706621

Released:
DOI: 10.2210/pdb5obr/pdb
PDB entry 5obr coloured by chain, front view.
PDB entry 5obr coloured by chain, side view.
PDB entry 5obr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase-TPX2 protein-protein interaction.
Cole DJ, Janecek M, Stokes JE, Rossmann M, Faver JC, McKenzie GJ, Venkitaraman AR, Hyvönen M, Spring DR, Huggins DJ, Jorgensen WL
Chem Commun (Camb) 53 9372-9375 (2017)
PMID: 28787041

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: 31.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O14965 (Residues: 125-391; Coverage: 66%)
Gene names: AIK, AIRK1, ARK1, AURA, AURKA, AYK1, BTAK, IAK1, STK15, STK6
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 9QT 1 x 9QT
Ligand SKE 1 x SKE
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P6122
Unit cell:
a: 83.7Å b: 83.7Å c: 169.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.223 0.292
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Aurora Kinase A Regulation by Cysteine Oxidative Modification.
Lee et al. (2023)
5 other articles

1 mention without citation

Discovery of Kinase and Carbonic Anhydrase Dual Inhibitors by Machine Learning Classification and Experiments.
Kim et al. (2022)