3DDU

Prolyl Oligopeptidase with GSK552

Summary for 3DDU

Entry DOI	10.2210/pdb3ddu/pdb
Descriptor	Prolyl endopeptidase, ACETATE ION, (6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)pyrrolo[1,2-a]pyrazin-4(6H)-one, ... (5 entities in total)
Functional Keywords	pop, prolyl oligopeptidase, endopeptidase, hydrolase
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm: P48147
Total number of polymer chains	1
Total formula weight	81455.20
Authors	Madauss, K.P.,Reid, R.A.,Haffner, C.D.,Miller, A.B. (deposition date: 2008-06-06, release date: 2008-08-19, Last modification date: 2024-02-21)
Primary citation	Haffner, C.D.,Diaz, C.J.,Miller, A.B.,Reid, R.A.,Madauss, K.P.,Hassell, A.,Hanlon, M.H.,Porter, D.J.,Becherer, J.D.,Carter, L.H. Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP) Bioorg.Med.Chem.Lett., 18:4360-4363, 2008 Cited by PubMed Abstract: We report the synthesis and in vitro activity of a series of novel pyrrolidinyl pyridones and pyrazinones as potent inhibitors of prolyl oligopeptidase (POP). Within this series, compound 39 was co-crystallized within the catalytic site of a human chimeric POP protein which provided a more detailed understanding of how these inhibitors interacted with the key residues within the catalytic pocket. PubMed: 18606544 DOI: 10.1016/j.bmcl.2008.06.067 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.56 Å)

Structure validation