› 4nts

X-ray diffraction
2.9Å resolution

Apo structure of the catalytic subunit of cAMP-dependent protein kinase

Released:
DOI: 10.2210/pdb4nts/pdb
PDB entry 4nts coloured by chain, front view.
PDB entry 4nts coloured by chain, side view.
PDB entry 4nts coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Molecular features of product release for the PKA catalytic cycle.
Bastidas AC, Wu J, Taylor SS
Biochemistry 54 2-10 (2015)
PMID: 25077557

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138536 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cAMP-dependent protein kinase catalytic subunit alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 350 amino acids
Theoretical weight: 40.63 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:

Ligands and Environments

1 bound ligand:
Ligand MYR 1 x MYR
2 modified residues:
Ligand TPO 2 x TPO
Ligand SEP 2 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21
Unit cell:
a: 50.96Å b: 142.61Å c: 63.16Å
α: 90° β: 103.65° γ: 90°
R-values:
R R work R free
0.247 0.244 0.292
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Evolution of a dynamic molecular switch.
Taylor et al. (2019)
2 more

8 mentions without citation

Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase's enzymatic cycle.
Wang et al. (2019)
7 more