› 3pna

X-ray diffraction
1.5Å resolution

Crystal Structure of cAMP bound (91-244)RIa Subunit of cAMP-dependent Protein Kinase

Released:
DOI: 10.2210/pdb3pna/pdb
PDB entry 3pna coloured by chain, front view.
PDB entry 3pna coloured by chain, side view.
PDB entry 3pna coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Cyclic AMP analog blocks kinase activation by stabilizing inactive conformation: conformational selection highlights a new concept in allosteric inhibitor design.
Badireddy S, Yunfeng G, Ritchie M, Akamine P, Wu J, Kim CW, Taylor SS, Qingsong L, Swaminathan K, Anand GS
Mol Cell Proteomics 10 M110.004390 (2011)
PMID: 21081668

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-132578 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed Chains: A, B
Molecule details ›
Chains: A, B
Length: 154 amino acids
Theoretical weight: 17.34 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00514 (Residues: 92-245; Coverage: 41%)
Gene name: PRKAR1A
Sequence domains: Cyclic nucleotide-binding domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand CMP 2 x CMP
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P3212
Unit cell:
a: 62.642Å b: 62.642Å c: 158.197Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.157 0.182
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Allosteric inhibition explained through conformational ensembles sampling distinct "mixed" states.
Byun et al. (2020)
4 more

4 mentions without citation

A tool set to map allosteric networks through the NMR chemical shift covariance analysis.
Boulton et al. (2014)
3 more