› 4g2l

X-ray diffraction
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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-131211 (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: Not provided
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 0WL 2 x 0WL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P41212
Unit cell:
a: 104.226Å b: 104.226Å c: 270.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.182 0.214
Expression system: Not provided

Quick links

Citations

7 review citations

Advances in targeting cyclic nucleotide phosphodiesterases.
Maurice et al. (2014)
6 more