› 3vap

X-ray diffraction
2.66Å resolution

Synthesis and SAR Studies of imidazo-[1,2-a]-pyrazine Aurora kinase inhibitors with improved off target kinase selectivity

Released:
DOI: 10.2210/pdb3vap/pdb
PDB entry 3vap coloured by chain, front view.
PDB entry 3vap coloured by chain, side view.
PDB entry 3vap coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Synthesis and SAR studies of imidazo-[1,2-a]-pyrazine Aurora kinase inhibitors with improved off-target kinase selectivity.
Voss ME, Rainka MP, Fleming M, Peterson LH, Belanger DB, Siddiqui MA, Hruza A, Voigt J, Gray K, Basso AD
Bioorg Med Chem Lett 22 3544-9 (2012)
PMID: 22503250

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: 31.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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

1 bound ligand:
Ligand 0FY 1 x 0FY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P6122
Unit cell:
a: 83.329Å b: 83.329Å c: 157.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.202 0.246
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Recent advances in development of imidazo[1,2-a]pyrazines: synthesis, reactivity and their biological applications.
Goel et al. (2015)
1 more