› 1lpu

X-ray diffraction
1.86Å resolution

Low Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays

Released:
DOI: 10.2210/pdb1lpu/pdb
PDB entry 1lpu coloured by chain, front view.
PDB entry 1lpu coloured by chain, side view.
PDB entry 1lpu coloured by chain, top view.
Source organism: Zea mays
Primary publication:
Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.
Yde CW, Ermakova I, Issinger OG, Niefind K
J Mol Biol 347 399-414 (2005)
PMID: 15740749

Function and Biology Details

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

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
UniProt:
  • Canonical: P28523 (Residues: 1-332; Coverage: 100%)
Gene name: ACK2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand BEN 1 x BEN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: C2
Unit cell:
a: 143.19Å b: 59.758Å c: 45.082Å
α: 90° β: 103.41° γ: 90°
R-values:
R R work R free
0.206 0.204 0.248
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Protein kinases CK1 and CK2 as new targets for neurodegenerative diseases.
Perez et al. (2011)
1 more

1 mention without citation

Inverse Mixed-Solvent Molecular Dynamics for Visualization of the Residue Interaction Profile of Molecular Probes.
Yanagisawa et al. (2022)