2ACL

Liver X-Receptor alpha Ligand Binding Domain with SB313987


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.220 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Discovery of substituted maleimides as liver x receptor agonists and determination of a ligand-bound crystal structure.

Jaye, M.C.Krawiec, J.A.Campobasso, N.Smallwood, A.Qiu, C.Lu, Q.Kerrigan, J.J.De Los Frailes Alvaro, M.Laffitte, B.Liu, W.S.Marino, J.P.Meyer, C.R.Nichols, J.A.Parks, D.J.Perez, P.Sarov-Blat, L.Seepersaud, S.D.Steplewski, K.M.Thompson, S.K.Wang, P.Watson, M.A.Webb, C.L.Haigh, D.Caravella, J.A.Macphee, C.H.Willson, T.M.Collins, J.L.

(2005) J Med Chem 48: 5419-5422

  • DOI: https://doi.org/10.1021/jm050532w
  • Primary Citation of Related Structures:  
    2ACL

  • PubMed Abstract: 

    Substituted 3-(phenylamino)-1H-pyrrole-2,5-diones were identified from a high throughput screen as inducers of human ATP binding cassette transporter A1 expression. Mechanism of action studies led to the identification of GSK3987 as an LXR ligand. GSK3987 recruits the steroid receptor coactivator-1 to human LXRalpha and LXRbeta with EC(50)s of 40 nM, profiles as an LXR agonist in functional assays, and activates LXR though a mechanism that is similar to first generation LXR agonists.


  • Organizational Affiliation

    GlaxoSmithKline Research and Development, Research Triangle Park, North Carolina 27709, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Retinoic acid receptor RXR-alpha
A, C, E, G
238Homo sapiensMutation(s): 0 
Gene Names: RXRANR2B1
UniProt & NIH Common Fund Data Resources
Find proteins for P19793 (Homo sapiens)
Explore P19793 
Go to UniProtKB:  P19793
PHAROS:  P19793
GTEx:  ENSG00000186350 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP19793
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Oxysterols receptor LXR-alpha
B, D, F, H
244Mus musculusMutation(s): 1 
Gene Names: Nr1h3Lxra
UniProt & NIH Common Fund Data Resources
Find proteins for Q9Z0Y9 (Mus musculus)
Explore Q9Z0Y9 
Go to UniProtKB:  Q9Z0Y9
IMPC:  MGI:1352462
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9Z0Y9
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
REA BindingDB:  2ACL IC50: min: 5.00e+4, max: 5.00e+4 (nM) from 3 assay(s)
L05 BindingDB:  2ACL EC50: 50 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.220 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.77α = 88.98
b = 81.95β = 75.2
c = 111.44γ = 78.27
Software Package:
Software NamePurpose
HKL-2000data collection
SCALEPACKdata scaling
AMoREphasing
CNXrefinement
HKL-2000data reduction

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-09-20
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Derived calculations