› 6q38

X-ray diffraction
1.74Å resolution

The Crystal structure of CK2a bound to P1-C4

Released:
DOI: 10.2210/pdb6q38/pdb
PDB entry 6q38 coloured by chain, front view.
PDB entry 6q38 coloured by chain, side view.
PDB entry 6q38 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Efficient development of stable and highly functionalised peptides targeting the CK2α/CK2β protein-protein interaction.
Iegre J, Brear P, Baker DJ, Tan YS, Atkinson EL, Sore HF, O' Donovan DH, Verma CS, Hyvönen M, Spring DR
Chem Sci 10 5056-5063 (2019)
PMID: 31183056

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-240870 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Casein kinase II subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 327 amino acids
Theoretical weight: 39.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P68400 (Residues: 3-329; Coverage: 84%)
Gene names: CK2A1, CSNK2A1
Sequence domains: Protein kinase domain
Structure domains:
Stapled Peptide Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.35 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand BEZ 1 x BEZ
Ligand A1H27 1 x A1H27
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21212
Unit cell:
a: 60.887Å b: 127.752Å c: 54.499Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.234
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

5 review citations

Role of CK2 inhibitor CX-4945 in anti-cancer combination therapy - potential clinical relevance.
D'Amore et al. (2020)
4 more

1 mention without citation

Efficient development of stable and highly functionalised peptides targeting the CK2α/CK2β protein-protein interaction.
Iegre et al. (2019)