3QQP

Crystal Structure of 11beta-Hydroxysteroid Dehydrogenase 1 (11b-HSD1) in Complex with Urea Inhibitor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.72 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.164 
  • R-Value Observed: 0.168 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Pyrrolidine-pyrazole ureas as potent and selective inhibitors of 11beta-hydroxysteroid-dehydrogenase type 1.

Venier, O.Pascal, C.Braun, A.Namane, C.Mougenot, P.Crespin, O.Pacquet, F.Mougenot, C.Monseau, C.Onofri, B.Dadji-Faihun, R.Leger, C.Ben-Hassine, M.Van-Pham, T.Ragot, J.L.Philippo, C.Gussregen, S.Engel, C.Farjot, G.Noah, L.Maniani, K.Nicolai, E.

(2011) Bioorg Med Chem Lett 21: 2244-2251

  • DOI: https://doi.org/10.1016/j.bmcl.2011.02.111
  • Primary Citation of Related Structures:  
    3QQP

  • PubMed Abstract: 

    A High Throughput Screening campaign allowed the identification of a novel class of ureas as 11β-HSD1 inhibitors. Rational chemical optimization provided potent and selective inhibitors of both human and murine 11β-HSD1 with an appropriate ADME profile and ex vivo activity in target tissues.


  • Organizational Affiliation

    Sanofi-aventis R&D, 1 Avenue Pierre Brossolette, 91385 Chilly-Mazarin, France. Olivier.Venier@sanofi-aventis.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Corticosteroid 11-beta-dehydrogenase isozyme 1
A, B, C, D
286Homo sapiensMutation(s): 1 
Gene Names: HSD11HSD11B1HSD11L
EC: 1.1.1.146
UniProt & NIH Common Fund Data Resources
Find proteins for P28845 (Homo sapiens)
Explore P28845 
Go to UniProtKB:  P28845
PHAROS:  P28845
GTEx:  ENSG00000117594 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP28845
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
S05 BindingDB:  3QQP IC50: 42 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.72 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.164 
  • R-Value Observed: 0.168 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 56.927α = 90
b = 153.385β = 93.46
c = 74.179γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
BUSTER-TNTrefinement
PDB_EXTRACTdata extraction
REFMACphasing
BUSTERrefinement

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-02-22
    Type: Initial release
  • Version 1.1: 2013-05-08
    Changes: Database references
  • Version 1.2: 2017-10-11
    Changes: Data collection
  • Version 1.3: 2024-02-21
    Changes: Data collection, Database references, Derived calculations