› 3qam

X-ray diffraction
1.92Å resolution

Crystal Structure of Glu208Ala mutant of catalytic subunit of cAMP-dependent protein kinase

Released:
DOI: 10.2210/pdb3qam/pdb
PDB entry 3qam coloured by chain, front view.
PDB entry 3qam coloured by chain, side view.
PDB entry 3qam coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
A conserved Glu-Arg salt bridge connects coevolved motifs that define the eukaryotic protein kinase fold.
Yang J, Wu J, Steichen JM, Kornev AP, Deal MS, Li S, Sankaran B, Woods VL, Taylor SS
J Mol Biol 415 666-79 (2012)
PMID: 22138346

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138546 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
cAMP-dependent protein kinase catalytic subunit alpha Chain: E
Molecule details ›
Chain: E
Length: 350 amino acids
Theoretical weight: 40.6 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P05132 (Residues: 2-351; Coverage: 100%)
Gene names: Pkaca, Prkaca
Sequence domains: Protein kinase domain
Structure domains:
cAMP-dependent protein kinase inhibitor alpha Chain: I
Molecule details ›
Chain: I
Length: 19 amino acids
Theoretical weight: 2.11 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P63248 (Residues: 6-24; Coverage: 25%)
Gene name: Pkia

Ligands and Environments

2 bound ligands:
Ligand ATP 1 x ATP
Ligand MG 2 x MG
2 modified residues:
Ligand TPO 1 x TPO
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21
Unit cell:
a: 48.412Å b: 79.639Å c: 60.8Å
α: 90° β: 113.28° γ: 90°
R-values:
R R work R free
0.195 0.195 0.228
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Dynamics-Driven Allostery in Protein Kinases.
Kornev et al. (2015)
3 more

4 mentions without citation

Role of N-terminal myristylation in the structure and regulation of cAMP-dependent protein kinase.
Bastidas et al. (2012)
3 more