3QK5

Crystal structure of fatty acid amide hydrolase with small molecule inhibitor

Summary for 3QK5

• Entry DOI: 10.2210/pdb3qk5/pdb
• Related: 3QJ8 3QJ9 3QKV
• Descriptor: Fatty-acid amide hydrolase 1, (3-{(3R)-1-[4-(1-benzothiophen-2-yl)pyrimidin-2-yl]piperidin-3-yl}-2-methyl-1H-pyrrolo[2,3-b]pyridin-1-yl)acetonitrile, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: protein-inhibitor complex, faah, fatty-acid amide hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Rattus norvegicus (rat)
• Cellular location: Endoplasmic reticulum membrane; Single-pass membrane protein: P97612
• Total number of polymer chains: 2
• Total formula weight: 131138.64

Authors

Min, X.,Walker, N.P.C.,Wang, Z. (deposition date: 2011-01-31, release date: 2011-04-06, Last modification date: 2023-09-13)

Primary citation

Gustin, D.J.,Ma, Z.,Min, X.,Li, Y.,Hedberg, C.,Guimaraes, C.,Porter, A.C.,Lindstrom, M.,Lester-Zeiner, D.,Xu, G.,Carlson, T.J.,Xiao, S.,Meleza, C.,Connors, R.,Wang, Z.,Kayser, F.
Identification of potent, noncovalent fatty acid amide hydrolase (FAAH) inhibitors.
Bioorg.Med.Chem.Lett., 21:2492-2496, 2011

PubMed Abstract: Starting from a series of ureas that were determined to be mechanism-based inhibitors of FAAH, several spirocyclic ureas and lactams were designed and synthesized. These efforts identified a series of novel, noncovalent FAAH inhibitors with in vitro potency comparable to known covalent FAAH inhibitors. The mechanism of action for these compounds was determined through a combination of SAR and co-crystallography with rat FAAH.

PubMed: 21392988
DOI: 10.1016/j.bmcl.2011.02.052

Experimental method

X-RAY DIFFRACTION (2.2 Å)