2GIU

Human estrogen receptor beta ligand-binding domain in complex with compound 45


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.323 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.227 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

The discovery of tetrahydrofluorenones as a new class of estrogen receptor beta-subtype selective ligands.

Wilkening, R.R.Ratcliffe, R.W.Tynebor, E.C.Wildonger, K.J.Fried, A.K.Hammond, M.L.Mosley, R.T.Fitzgerald, P.M.D.Sharma, N.McKeever, B.M.Nilsson, S.Carlquist, M.Thorsell, A.Locco, L.Katz, R.Frisch, K.Birzin, E.T.Wilkinson, H.A.Mitra, S.Cai, S.Hayes, E.C.Schaeffer, J.M.Rohrer, S.P.

(2006) Bioorg Med Chem Lett 16: 3489-3494

  • DOI: https://doi.org/10.1016/j.bmcl.2006.03.098
  • Primary Citation of Related Structures:  
    2GIU

  • PubMed Abstract: 

    Synthesis and derivatization of a series of substituted tetrahydrofluorenone analogs giving potent, ERbeta subtype selective ligands are described. Several analogs possessing ERbeta binding affinities comparable to 17beta-estradiol but with greater than 75-fold selectivity over ERalpha are reported.


  • Organizational Affiliation

    Department of Medicinal Chemistry, Merck Research Laboratories, PO Box 2000, Rahway, NJ 07065, USA. robert_wilkening@merck.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Estrogen receptor beta241Homo sapiensMutation(s): 0 
Gene Names: ESR2
UniProt & NIH Common Fund Data Resources
Find proteins for Q92731 (Homo sapiens)
Explore Q92731 
Go to UniProtKB:  Q92731
PHAROS:  Q92731
GTEx:  ENSG00000140009 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ92731
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
FBR
Query on FBR

Download Ideal Coordinates CCD File 
B [auth A](9aS)-4-bromo-9a-butyl-7-hydroxy-1,2,9,9a-tetrahydro-3H-fluoren-3-one
C17 H19 Br O2
FTEBGBCQCYMDPH-KRWDZBQOSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
FBR PDBBind:  2GIU IC50: 1.5 (nM) from 1 assay(s)
BindingDB:  2GIU IC50: min: 1.5, max: 1.8 (nM) from 2 assay(s)
EC50: 4 (nM) from 1 assay(s)
Binding MOAD:  2GIU IC50: 1.5 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.323 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.227 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.53α = 90
b = 64.53β = 90
c = 251.16γ = 120
Software Package:
Software NamePurpose
X-GENdata scaling
X-GENdata reduction
SHELXLrefinement
MAR345data collection

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-10-10
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Refinement description
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references, Derived calculations