› 1ds5

X-ray diffraction
3.16Å resolution

DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.

Released:
DOI: 10.2210/pdb1ds5/pdb
PDB entry 1ds5 coloured by chain, front view.
PDB entry 1ds5 coloured by chain, side view.
PDB entry 1ds5 coloured by chain, top view.
Source organisms:
Primary publication:
The crystal structure of the complex of Zea mays alpha subunit with a fragment of human beta subunit provides the clue to the architecture of protein kinase CK2 holoenzyme.
Battistutta R, Sarno S, De Moliner E, Marin O, Issinger OG, Zanotti G, Pinna LA
Eur J Biochem 267 5184-90 (2000)
PMID: 10931203

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:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151245 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Casein kinase II subunit alpha Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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:
Casein kinase II subunit beta Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 23 amino acids
Theoretical weight: 2.77 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P67870 (Residues: 181-203; Coverage: 11%)
Gene names: CK2N, CSNK2B, G5A

Ligands and Environments

2 bound ligands:
Ligand AMP 4 x AMP
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P212121
Unit cell:
a: 87.681Å b: 119.846Å c: 145.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.289
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

Survey of the year 2000 commercial optical biosensor literature.
Rich et al. (2001)
15 other articles

5 mentions without citation

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