› 4rlk

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

Released:
DOI: 10.2210/pdb4rlk/pdb
PDB entry 4rlk coloured by chain, front view.
PDB entry 4rlk coloured by chain, side view.
PDB entry 4rlk coloured by chain, top view.
Source organism: Zea mays
Primary publication:
Protein kinase CK2 inhibition is associated with the destabilization of HIF-1α in human cancer cells.
Guerra B, Rasmussen TD, Schnitzler A, Jensen HH, Boldyreff BS, Miyata Y, Marcussen N, Niefind K, Issinger OG
Cancer Lett 356 751-61 (2015)
PMID: 25449433

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151243 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • Canonical: P28523 (Residues: 1-332; Coverage: 100%)
Gene name: ACK2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand GOL 3 x GOL
Ligand ACT 2 x ACT
Ligand E91 1 x E91
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-values:
R R work R free
0.145 0.143 0.175
Expression system: Escherichia coli BL21(DE3)

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Citations

8 review citations

CK2-An Emerging Target for Neurological and Psychiatric Disorders.
Castello et al. (2017)
7 more