6BQ0

Structure of human monoacylglycerol lipase bound to a covalent inhibitor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.214 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.180 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Discovery of Trifluoromethyl Glycol Carbamates as Potent and Selective Covalent Monoacylglycerol Lipase (MAGL) Inhibitors for Treatment of Neuroinflammation.

McAllister, L.A.Butler, C.R.Mente, S.O'Neil, S.V.Fonseca, K.R.Piro, J.R.Cianfrogna, J.A.Foley, T.L.Gilbert, A.M.Harris, A.R.Helal, C.J.Johnson, D.S.Montgomery, J.I.Nason, D.M.Noell, S.Pandit, J.Rogers, B.N.Samad, T.A.Shaffer, C.L.da Silva, R.G.Uccello, D.P.Webb, D.Brodney, M.A.

(2018) J Med Chem 61: 3008-3026

  • DOI: https://doi.org/10.1021/acs.jmedchem.8b00070
  • Primary Citation of Related Structures:  
    6BQ0

  • PubMed Abstract: 

    Monoacylglycerol lipase (MAGL) inhibition provides a potential treatment approach to neuroinflammation through modulation of both the endocannabinoid pathway and arachidonoyl signaling in the central nervous system (CNS). Herein we report the discovery of compound 15 (PF-06795071), a potent and selective covalent MAGL inhibitor, featuring a novel trifluoromethyl glycol leaving group that confers significant physicochemical property improvements as compared with earlier inhibitor series with more lipophilic leaving groups. The design strategy focused on identifying an optimized leaving group that delivers MAGL potency, serine hydrolase selectivity, and CNS exposure while simultaneously reducing log  D, improving solubility, and minimizing chemical lability. Compound 15 achieves excellent CNS exposure, extended 2-AG elevation effect in vivo, and decreased brain inflammatory markers in response to an inflammatory challenge.


  • Organizational Affiliation

    Pfizer Worldwide Research and Development , 610 Main Street , Cambridge , Massachusetts 02139 , United States.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Monoglyceride lipase
A, B
348Homo sapiensMutation(s): 0 
Gene Names: MGLL
EC: 3.1.1.23
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for Q99685 (Homo sapiens)
Explore Q99685 
Go to UniProtKB:  Q99685
PHAROS:  Q99685
GTEx:  ENSG00000074416 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ99685
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
E3A (Subject of Investigation/LOI)
Query on E3A

Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]
1-({(1R,5S,6r)-6-[1-(4-fluorophenyl)-1H-pyrazol-3-yl]-3-azabicyclo[3.1.0]hexane-3-carbonyl}oxy)pyrrolidine-2,5-dione
C19 H17 F N4 O4
FNIBKVOGYHDUDM-UOIKSKOESA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.214 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.180 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 86.31α = 90
b = 126.62β = 90
c = 138.06γ = 90
Software Package:
Software NamePurpose
HKL-2000data scaling
BUSTERrefinement
PDB_EXTRACTdata extraction
HKL-2000data reduction
BUSTERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

  • Released Date: 2018-03-14 
  • Deposition Author(s): Pandit, J.

Revision History  (Full details and data files)

  • Version 1.0: 2018-03-14
    Type: Initial release
  • Version 1.1: 2018-04-25
    Changes: Data collection, Database references
  • Version 1.2: 2023-10-04
    Changes: Data collection, Database references, Refinement description