1HJ1

RAT OESTROGEN RECEPTOR BETA LIGAND-BINDING DOMAIN IN COMPLEX WITH PURE ANTIOESTROGEN ICI164,384

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.251 
  • R-Value Work: 0.220 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history. 


Literature

Structural Insights Into the Mode of Action of a Pure Antiestrogen

Pike, A.C.W., Brzozowski, A.M., Walton, J., Hubbard, R.E., Thorsell, A.G., Li, Y.L., Gustafsson, J.A., Carlquist, M.

(2001) Structure 9: 145

  • DOI: https://doi.org/10.1016/s0969-2126(01)00568-8
  • Primary Citation of Related Structures:  
    1HJ1

  • PubMed Abstract: 

    Estrogens exert their effects on target tissues by binding to a nuclear transcription factor termed the estrogen receptor (ER). Previous structural studies have demonstrated that each class of ER ligand (agonist, partial agonist, and SERM antagonist) induces distinctive orientations in the receptor's carboxy-terminal transactivation helix. The conformation of this portion of the receptor determines whether ER can recruit and interact with the components of the transcriptional machinery, thereby facilitating target gene expression.

    • Organizational Affiliation: 

    Structural Biology Laboratory, Chemistry Department, University of York, Heslington, YO10 5DD, York, United Kingdom.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
OESTROGEN RECEPTOR BETA255Rattus norvegicusMutation(s): 0 
Gene Names: OESTROGEN RECEPTOR BETA
UniProt
Find proteins for Q62986 (Rattus norvegicus)
Explore Q62986 
Go to UniProtKB:  Q62986
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ62986
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
AOE
Query on AOE
Download Ideal Coordinates CCD File 
B [auth A]N-BUTYL-11-[(7R,8R,9S,13S,14S,17S)-3,17-DIHYDROXY-13-METHYL-7,8,9,11,12,13,14,15,16,17-DECAHYDRO-6H-CYCLOPENTA[A]PHENANTHREN-7-YL]-N-METHYLUNDECANAMIDE
C34 H55 N O3
BVVFOLSZMQVDKV-KXQIQQEYSA-N
PMB
Query on PMB
Download Ideal Coordinates CCD File 
C [auth A]PARA-MERCURY-BENZENESULFONIC ACID
C6 H5 Hg O3 S
KQAOIKIZSJJTII-UHFFFAOYSA-N
NI
Query on NI
Download Ideal Coordinates CCD File 
D [auth A],
E [auth A]		NICKEL (II) ION
Ni
VEQPNABPJHWNSG-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
AOE BindingDB:  1HJ1 Ki: min: 1.5, max: 4.6 (nM) from 4 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.251 
  • R-Value Work: 0.220 
  • Space Group: I 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.38α = 90
b = 82.67β = 90
c = 106.34γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CCP4phasing
REFMACrefinement

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-01-04
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-10-24
    Changes: Data collection, Source and taxonomy
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description