› 5oni

X-ray diffraction
2Å resolution

LOW-SALT STRUCTURE OF PROTEIN KINASE CK2 CATALYTIC SUBUNIT (ISOFORM CK2ALPHA) IN COMPLEX WITH THE INDENOINDOLE-TYPE INHIBITOR 4P

Released:
DOI: 10.2210/pdb5oni/pdb
PDB entry 5oni coloured by chain, front view.
PDB entry 5oni coloured by chain, side view.
PDB entry 5oni coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Unexpected Binding Mode of a Potent Indeno[1,2-b]indole-Type Inhibitor of Protein Kinase CK2 Revealed by Complex Structures with the Catalytic Subunit CK2α and Its Paralog CK2α'.
Hochscherf J, Lindenblatt D, Witulski B, Birus R, Aichele D, Marminon C, Bouaziz Z, Le Borgne M, Jose J, Niefind K
Pharmaceuticals (Basel) 10 (2017)
PMID: 29236079

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-159383 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Casein kinase II subunit alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 391 amino acids
Theoretical weight: 45.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P68400 (Residues: 1-391; Coverage: 100%)
Gene names: CK2A1, CSNK2A1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand 9YE 2 x 9YE
Ligand SO4 10 x SO4
Ligand NA 1 x NA
Ligand CL 2 x CL
Ligand BU1 1 x BU1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P43212
Unit cell:
a: 128.453Å b: 128.453Å c: 124.106Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.175 0.204
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Diacritic Binding of an Indenoindole Inhibitor by CK2α Paralogs Explored by a Reliable Path to Atomic Resolution CK2α' Structures.
Lindenblatt et al. (2019)
3 more

1 mention without citation

Unexpected Binding Mode of a Potent Indeno[1,2-b]indole-Type Inhibitor of Protein Kinase CK2 Revealed by Complex Structures with the Catalytic Subunit CK2α and Its Paralog CK2α'.
Hochscherf et al. (2017)