› 5zn1

X-ray diffraction
1.05Å resolution

X-ray structure of protein kinase ck2 alpha subunit in D2O

Released:
DOI: 10.2210/pdb5zn1/pdb
PDB entry 5zn1 coloured by chain, front view.
PDB entry 5zn1 coloured by chain, side view.
PDB entry 5zn1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Hydration Structures of the Human Protein Kinase CK2α Clarified by Joint Neutron and X-ray Crystallography.
Shibazaki C, Arai S, Shimizu R, Saeki M, Kinoshita T, Ostermann A, Schrader TE, Kurosaki Y, Sunami T, Kuroki R, Adachi M
J Mol Biol 430 5094-5104 (2018)
PMID: 30359582

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-159383 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Casein kinase II subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 39.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P68400 (Residues: 1-329; Coverage: 84%)
Gene names: CK2A1, CSNK2A1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand DOD 478 x DOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 58.641Å b: 45.543Å c: 63.546Å
α: 90° β: 111.79° γ: 90°
R-values:
R R work R free
0.161 0.16 0.18
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Copper Modulates the Catalytic Activity of Protein Kinase CK2.
Chojnowski et al. (2022)
1 more

1 mention without citation

Nano and micro reoriented domains and their relation with the crystal structure in the New Fe1.5Zn1.5B7O13Cl boracite.
Ulloa-Godínez et al. (2011)