› 4ceg

X-ray diffraction
2.1Å resolution

Crystal structure of Aurora A 122-403 C290A, C393A bound to ADP

Released:
DOI: 10.2210/pdb4ceg/pdb
PDB entry 4ceg coloured by chain, front view.
PDB entry 4ceg coloured by chain, side view.
PDB entry 4ceg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of C290A:C393A Aurora A provides structural insights into kinase regulation.
Burgess SG, Bayliss R
Acta Crystallogr F Struct Biol Commun 71 315-9 (2015)
PMID: 25760707

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: 285 amino acids
Theoretical weight: 32.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O14965 (Residues: 122-403; Coverage: 70%)
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 GOL 2 x GOL
Ligand MG 2 x MG
Ligand CL 4 x CL
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: 80.95Å b: 80.95Å c: 174.53Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.2 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Insights into the non-mitotic functions of Aurora kinase A: more than just cell division.
Bertolin et al. (2020)
1 more

7 mentions without citation

Structural basis of N-Myc binding by Aurora-A and its destabilization by kinase inhibitors.
Richards et al. (2016)
6 more