› 5w6e

X-ray diffraction
1.9Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169511 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B Chain: A
Molecule details ›
Chain: A
Length: 369 amino acids
Theoretical weight: 42.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q01064 (Residues: 142-507; Coverage: 68%)
Gene names: PDE1B, PDES1B
Sequence domains: 3'5'-cyclic nucleotide phosphodiesterase
Structure domains: 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand MG 1 x MG
Ligand 0NY 1 x 0NY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P43212
Unit cell:
a: 88.782Å b: 88.782Å c: 134.806Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.206
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Role of phosphodiesterase 1 in the pathophysiology of diseases and potential therapeutic opportunities.
Samidurai et al. (2021)
5 other articles

1 mention without citation

Enzyme Inhibitory Activities of Extracts and Carpachromene from the Stem of Ficus benghalensis.
Rauf et al. (2022)