› 1zxa

Solution NMR

Solution Structure of the Coiled-Coil Domain of cGMP-dependent Protein Kinase Ia

Released:
DOI: 10.2210/pdb1zxa/pdb
PDB entry 1zxa coloured by chain, ensemble of 20 models, front view.
PDB entry 1zxa coloured by chain, ensemble of 20 models, side view.
PDB entry 1zxa coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.
Schnell JR, Zhou GP, Zweckstetter M, Rigby AC, Chou JJ
Protein Sci 14 2421-8 (2005)
PMID: 16131665

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171845 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cGMP-dependent protein kinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 67 amino acids
Theoretical weight: 7.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13976 (Residues: 2-59; Coverage: 9%)
Gene names: PRKG1, PRKG1B, PRKGR1A, PRKGR1B
Sequence domains: Coiled-coil N-terminus of cGMP-dependent protein kinase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, RDC refinement and analysis
Expression system: Escherichia coli

Quick links

Citations

3 review citations

IRAG and novel PKG targeting in the cardiovascular system.
Schlossmann et al. (2011)
2 more

6 mentions without citation

Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase.
Sharma et al. (2008)
5 more