PDEStrIAn: A Phosphodiesterase Structure and Ligand Interaction Annotated Database As a Tool for Structure-Based Drug Design

Dataset OPEN
Jansen, Chimed; Kooistra, Albert J.; Kanev, Georgi K.; Leurs, Rob; J. P. de Esch, Iwan; Graaf, Chris de;
(2016)
  • Publisher: Figshare
  • Related identifiers: doi: 10.1021/acs.jmedchem.5b01813.s001, doi: 10.5281/zenodo.45774
  • Subject: Molecular Biology | Biotechnology | zenodo | Phosphodiesterase Structure | domain crystal structures | 57 PDE ligand binding site residues | crystal structures | future drug discovery studies | PDE interaction | Protein Data Bank | PDEs | Pharmacology | phosphodiesterases | ligand interaction | Biophysics | PDE ligands | chemical scaffolds | structure-based drug design | substructure analysis | drug design | PDE binding | Uncategorized | Medicine | binding modes | ChEMBL database | cocrystallized PDE ligands | PDB | IFP | 220 phosphodiesterase | Biochemistry | ligand design | Ligand Interaction Annotated Database
    • FOR: 80699 Information Systems not elsewhere classified | 110309 Infectious Diseases | 60506 Virology | 39999 Chemical Sciences not elsewhere classified
    mesheuropmc: enzymes and coenzymes (carbohydrates) | circulatory and respiratory physiology | sense organs | musculoskeletal system | heterocyclic compounds

<p>A systematic analysis is presented of the 220 phosphodiesterase (PDE) catalytic domain crystal structures present in the Protein Data Bank (PDB) with a focus on PDE-ligand interactions. The consistent structural alignment of 57 PDE ligand binding site residues enable... View more
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