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PDBsum entry 1zaf
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protein ligands Protein-protein interface(s) links
Transcription/transferase PDB id
1zaf

 

 

 

 

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Contents
Protein chains
228 a.a. *
13 a.a. *
Ligands
789 ×2
Waters ×167
* Residue conservation analysis
PDB id:
1zaf
Name: Transcription/transferase
Title: Crystal structure of estrogen receptor beta complexed with 3-bromo-6- hydroxy-2-(4-hydroxy-phenyl)-inden-1-one
Structure: Estrogen receptor beta. Chain: a, b. Synonym: er-beta. Engineered: yes. Nuclear receptor coactivator 1. Chain: c, d. Synonym: ncoa-1, steroid receptor coactivator-1, src-1, rip160, hin-2 protein. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: esr2, estrb, nr3a2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: this sequence was derived from steroid receptor coactivator-1.
Biol. unit: Tetramer (from PQS)
Resolution:
2.20Å     R-factor:   0.226     R-free:   0.286
Authors: R.E.Mcdevitt,M.S.Malamas,E.S.Manas,R.J.Unwalla,Z.B.Xu,C.P.Miller, H.A.Harris
Key ref: R.E.McDevitt et al. (2005). Estrogen receptor ligands: design and synthesis of new 2-arylindene-1-ones. Bioorg Med Chem Lett, 15, 3137-3142. PubMed id: 15876535 DOI: 10.1016/j.bmcl.2005.04.013
Date:
06-Apr-05     Release date:   11-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q92731  (ESR2_HUMAN) -  Estrogen receptor beta from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		530 a.a.
228 a.a.*
Protein chains
Pfam   ArchSchema ?
Q15788  (NCOA1_HUMAN) -  Nuclear receptor coactivator 1 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1441 a.a.
13 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains C, D: E.C.2.3.1.48  - histone acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-lysyl-[protein] + acetyl-CoA = N6-acetyl-L-lysyl-[protein] + CoA + H+
L-lysyl-[protein]
 + acetyl-CoA
 = N(6)-acetyl-L-lysyl-[protein]
 + CoA
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1016/j.bmcl.2005.04.013 Bioorg Med Chem Lett 15:3137-3142 (2005)
PubMed id: 15876535  
 
 
Estrogen receptor ligands: design and synthesis of new 2-arylindene-1-ones.
R.E.McDevitt, M.S.Malamas, E.S.Manas, R.J.Unwalla, Z.B.Xu, C.P.Miller, H.A.Harris.
 
  ABSTRACT  
 
The syntheses of a series of 2-arylindene-1-ones as potent ligands of ERbeta and ERalpha are described. Several compounds exhibited high potency and moderate selectivity for the ERbeta receptor. X-ray and modeling studies were used to understand ligand binding orientation and observed affinity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19967775 F.Minutolo, M.Macchia, B.S.Katzenellenbogen, and J.A.Katzenellenbogen (2011).
Estrogen receptor β ligands: Recent advances and biomedical applications.
  Med Res Rev, 31, 364-442.  
16914190 P.Ascenzi, A.Bocedi, and M.Marino (2006).
Structure-function relationship of estrogen receptor alpha and beta: impact on human health.
  Mol Aspects Med, 27, 299-402.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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