X-ray diffraction
1.24Å resolution

Crystal structure of Z. mays CK2alpha in complex with the ATP-competitive inhibitor 4-[(E)-(fluoren-9-ylidenehydrazinylidene)-methyl] benzoate


Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Casein kinase II subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 332 amino acids
Theoretical weight: 39.29 KDa
Source organism: Zea mays
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P28523 (Residues: 1-332; Coverage: 100%)
Gene name: ACK2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: C2
Unit cell:
a: 142.748Å b: 59.683Å c: 44.884Å
α: 90° β: 102.96° γ: 90°
R R work R free
0.145 0.143 0.175
Expression system: Escherichia coli BL21(DE3)