› 1lp4

X-ray diffraction
1.86Å resolution

Crystal structure of a binary complex of the catalytic subunit of protein kinase CK2 with Mg-AMPPNP

Released:
DOI: 10.2210/pdb1lp4/pdb
PDB entry 1lp4 coloured by chain, front view.
PDB entry 1lp4 coloured by chain, side view.
PDB entry 1lp4 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 BL21(DE3)
UniProt:
  • Canonical: P28523 (Residues: 1-332; Coverage: 100%)
Gene name: ACK2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand ANP 1 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: C2
Unit cell:
a: 144.075Å b: 59.624Å c: 45.642Å
α: 90° β: 103.59° γ: 90°
R-values:
R R work R free
0.207 0.206 0.244
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

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

9 mentions without citation

Substrate and docking interactions in serine/threonine protein kinases.
Goldsmith et al. (2007)
8 more