› 1ol6

X-ray diffraction
3Å resolution

Structure of unphosphorylated D274N mutant of Aurora-A

Released:
DOI: 10.2210/pdb1ol6/pdb
PDB entry 1ol6 coloured by chain, front view.
PDB entry 1ol6 coloured by chain, side view.
PDB entry 1ol6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of Aurora-A activation by TPX2 at the mitotic spindle.
Bayliss R, Sardon T, Vernos I, Conti E
Mol Cell 12 851-62 (2003)
PMID: 14580337

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

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: 282 amino acids
Theoretical weight: 32.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

1 bound ligand:
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P41212
Unit cell:
a: 87.31Å b: 87.31Å c: 77.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.277 0.277 0.301
Expression system: Escherichia coli

Quick links

Citations

82 review citations

Regulation of protein kinases; controlling activity through activation segment conformation.
Nolen et al. (2004)
81 more

6 mentions without citation

Boosting the Full Potential of PyMOL with Structural Biology Plugins.
Rosignoli et al. (2022)
5 more