› 3jsw

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
Guanosine 3',5'-cyclic phosphate + H(2)O = guanosine 5'-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131212 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A Chains: A, B
Molecule details ›
Chains: A, B
Length: 329 amino acids
Theoretical weight: 38.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O76083 (Residues: 242-566; Coverage: 55%)
Gene name: PDE9A
Sequence domains: 3'5'-cyclic nucleotide phosphodiesterase
Structure domains: 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand MG 2 x MG
Ligand JAR 2 x JAR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P41212
Unit cell:
a: 103.278Å b: 103.278Å c: 270.349Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.18 0.212
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Mammalian cyclic nucleotide phosphodiesterases: molecular mechanisms and physiological functions.
Francis et al. (2011)
4 more

2 mentions without citation

A Perspective on Natural and Nature-Inspired Small Molecules Targeting Phosphodiesterase 9 (PDE9): Chances and Challenges against Neurodegeneration.
Ribaudo et al. (2021)
1 more