PDBe 4qx5

X-ray diffraction
1.32Å resolution

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

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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%)
  • Best match: Q13976-3 (Residues: 16-72)
Gene names: PRKG1, PRKG1B, PRKGR1A, PRKGR1B
Sequence domains: Cyclic nucleotide-binding domain
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:

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