› 4qx5

X-ray diffraction
1.32Å resolution

Neutron diffraction reveals hydrogen bonds critical for cGMP-selective activation: Insights for PKG agonist design

Released:
DOI: 10.2210/pdb4qx5/pdb
PDB entry 4qx5 coloured by chain, front view.
PDB entry 4qx5 coloured by chain, side view.
PDB entry 4qx5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Neutron diffraction reveals hydrogen bonds critical for cGMP-selective activation: insights for cGMP-dependent protein kinase agonist design.
Huang GY, Gerlits OO, Blakeley MP, Sankaran B, Kovalevsky AY, Kim C
Biochemistry 53 6725-7 (2014)
PMID: 25271401

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171844 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cGMP-dependent protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 16.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13976 (Residues: 204-354; Coverage: 23%)
Gene names: PRKG1, PRKG1B, PRKGR1A, PRKGR1B
Sequence domains: Cyclic nucleotide-binding domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand CMP 1 x CMP
Ligand IOD 18 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P41212
Unit cell:
a: 48.44Å b: 48.44Å c: 103.462Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.224
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

2 mentions without citation

Neutron diffraction reveals hydrogen bonds critical for cGMP-selective activation: insights for cGMP-dependent protein kinase agonist design.
Huang et al. (2014)
1 more