PDBe 3e3b

X-ray diffraction
3.2Å resolution

Crystal structure of catalytic subunit of human protein kinase CK2alpha prime with a potent indazole-derivative inhibitor

Released:
Source organism: Homo sapiens
Primary publication:
Structure of human protein kinase CK2 alpha 2 with a potent indazole-derivative inhibitor.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 75-9 (2009)
PMID: 19193990

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Casein kinase II subunit alpha' Chain: X
Molecule details ›
Chain: X
Length: 339 amino acids
Theoretical weight: 40.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19784 (Residues: 1-334; Coverage: 95%)
Gene names: CK2A2, CSNK2A2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21212
Unit cell:
a: 69.813Å b: 102.126Å c: 46.618Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.268 0.248 0.274
Expression system: Escherichia coli