2hwn

X-ray diffraction
1.6Å resolution

Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide

Released:

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero hexamer
PDBe Complex ID:
PDB-CPX-146153 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
cAMP-dependent protein kinase type II-alpha regulatory subunit Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 45 amino acids
Theoretical weight: 5.29 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12368 (Residues: 1-45; Coverage: 11%)
Gene name: Prkar2a
Sequence domains: Regulatory subunit of type II PKA R-subunit
Structure domains: cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain
RGS domain-containing protein Chains: E, F
Molecule details ›
Chains: E, F
Length: 22 amino acids
Theoretical weight: 2.61 KDa
Source organism: Macaca fascicularis
Expression system: Not provided
UniProt:
  • Canonical: Q4R5S0 (Residues: 605-625; Coverage: 3%)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: C2
Unit cell:
a: 99.551Å b: 44.561Å c: 72.802Å
α: 90° β: 124.07° γ: 90°
R-values:
R R work R free
0.21 0.208 0.239
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided