Reaction Details Report a problem with these data
Target
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Ligand
BDBM50048272
Substrate
n/a
Meas. Tech.
ChEMBL_1458263 (CHEMBL3368978)
IC50
90±n/a nM
Citation
 Das, S; Shelke, DE; Harde, RL; Avhad, VB; Khairatkar-Joshi, N; Gullapalli, S; Gupta, PK; Gandhi, MN; Bhateja, DK; Bajpai, M; Joshi, AA; Marathe, MY; Gudi, GS; Jadhav, SB; Mahat, MY; Thomas, A Design, synthesis and pharmacological evaluation of novel polycyclic heteroarene ethers as PDE10A inhibitors: part II. Bioorg Med Chem Lett 24:3238-42 (2014) [PubMed]  Article 
Target
Name:
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Synonyms:
PDE10_RAT | Pde10a | Phosphodiesterase 10 | Phosphodiesterase 10A (PDE10A2) | Phosphodiesterase Type 10 (PDE10A) | Rat recombinant PDE10a (rPDE10a)
Type:
Enzyme
Mol. Mass.:
90160.88
Organism:
Rattus norvegicus (rat)
Description:
PDE10A was generated from the full-length recombinant rat clone transfected into Sf9 cells.
Residue:
794
Sequence:
MEDGPSNNASCFRRLTECFLSPSLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKNNKAEDEPSPKEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGPITQGTTISAYVAKSRKTLLVEDILGDERFPRGTGLESGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVCRGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIRHSECIYRVTMEKLSYHSICTSEEWQGLMHFNLPARICRDIELFHFDIGPFENMWPGIFVYMIHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNNGLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLHNQSHRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLNQWEKVIRGEETAMWISGPATSKSTSEKPTRKVDD
  
Inhibitor
Name:
BDBM50048272
Synonyms:
CHEMBL3315034
Type:
Small organic molecule
Emp. Form.:
C26H18N6O
Mol. Mass.:
430.4607
SMILES:
Cn1cc(-c2cccc(Oc3nccc(n3)-c3cncnc3)c2)c2nc3ccccc3cc12
Structure:
Search PDB for entries with ligand similarity: