X-ray diffraction
2.1Å resolution

Crystal structure of the catalytic domain of PDE4D2 with (S)-N-(3-{1-[1-(3-Cyclopropylmethoxy-4-difluoromethoxyphenyl)-2-(1-oxypyridin-4-yl)-ethyl]-1H-pyrazl-3-yl}phenyl)acetamide

Source organism: Homo sapiens
Entry authors: Kim HT, Chang HJ

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
cAMP-specific 3',5'-cyclic phosphodiesterase 4D Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 360 amino acids
Theoretical weight: 41.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q08499 (Residues: 381-740; Coverage: 45%)
Gene names: DPDE3, PDE4D
Sequence domains: 3'5'-cyclic nucleotide phosphodiesterase
Structure domains: 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: P212121
Unit cell:
a: 98.587Å b: 110.293Å c: 161.607Å
α: 90° β: 90° γ: 90°
R R work R free
0.208 0.206 0.236
Expression system: Escherichia coli