› 3u87

X-ray diffraction
2.9Å resolution

Structure of a chimeric construct of human CK2alpha and human CK2alpha' in complex with a non-hydrolysable ATP-analogue

Released:
DOI: 10.2210/pdb3u87/pdb
PDB entry 3u87 coloured by chain, front view.
PDB entry 3u87 coloured by chain, side view.
PDB entry 3u87 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Low-density crystal packing of human protein kinase CK2 catalytic subunit in complex with resorufin or other ligands: a tool to study the unique hinge-region plasticity of the enzyme without packing bias.
Klopffleisch K, Issinger OG, Niefind K
Acta Crystallogr D Biol Crystallogr 68 883-92 (2012)
PMID: 22868753

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-148707 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Casein kinase II subunit alpha; Casein kinase II subunit alpha' Chains: A, B
Molecule details ›
Chains: A, B
Length: 349 amino acids
Theoretical weight: 41.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19784 (Residues: 1-1, 327-350; Coverage: 7%)
  • Canonical: P68400 (Residues: 2-325; Coverage: 83%)
Gene names: CK2A1, CK2A2, CSNK2A1, CSNK2A2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ANP 2 x ANP
Ligand MG 4 x MG
Ligand CL 2 x CL
Ligand SO4 2 x SO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P43212
Unit cell:
a: 127.821Å b: 127.821Å c: 125.333Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.218
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Role of Computational Methods in Going beyond X-ray Crystallography to Explore Protein Structure and Dynamics.
Srivastava et al. (2018)
9 other articles

1 mention without citation

Coupling Supervised Molecular Dynamics (SuMD) with Entropy Estimations To Shine Light on the Stability of Multiple Binding Sites.
Panday et al. (2019)