› 5tkb

X-ray diffraction
2.16Å resolution

Function and Biology Details

Reaction catalysed: 
Adenosine 3',5'-cyclic phosphate + H(2)O = adenosine 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-170654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3',5'-cyclic-AMP phosphodiesterase 4D Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 381 amino acids
Theoretical weight: 43.79 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q08499 (Residues: 380-753; Coverage: 46%)
Gene names: DPDE3, PDE4D
Sequence domains: 3'5'-cyclic nucleotide phosphodiesterase
Structure domains: 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain

Ligands and Environments

5 bound ligands:
Ligand ZN 4 x ZN
Ligand MG 4 x MG
Ligand SO4 3 x SO4
Ligand EOH 8 x EOH
Ligand 7DJ 4 x 7DJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 99Å b: 112.7Å c: 159.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.188 0.209
Expression system: Spodoptera frugiperda

Quick links

Citations

9 review citations

Prospects for pharmacological targeting of pseudokinases.
Kung et al. (2019)
8 more

2 mentions without citation

Identification of imidazo[1,2-b]pyridazine TYK2 pseudokinase ligands as potent and selective allosteric inhibitors of TYK2 signalling.
Moslin et al. (2017)
1 more