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PDBsum entry 4a69

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protein ligands metals Protein-protein interface(s) links
Transcription PDB id
4a69
Jmol
Contents
Protein chains
369 a.a.
69 a.a.
Ligands
ACT ×2
GOL ×4
I0P ×2
Metals
_ZN ×2
__K ×4
Waters ×347
PDB id:
4a69
Name: Transcription
Title: Structure of hdac3 bound to corepressor and inositol tetraph
Structure: Histone deacetylase 3,. Chain: a, b. Fragment: residues 1-376. Synonym: hd3, rpd3-2, smap45, hdac3. Engineered: yes. Nuclear receptor corepressor 2. Chain: c, d. Fragment: residues 389-480. Synonym: n-cor2, ctg repeat protein 26, smap270, silencing
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293f.
Resolution:
2.06Å     R-factor:   0.189     R-free:   0.236
Authors: P.J.Watson,L.Fairall,G.M.Santos,J.W.R.Schwabe
Key ref: P.J.Watson et al. (2012). Structure of HDAC3 bound to co-repressor and inositol tetraphosphate. Nature, 481, 335-340. PubMed id: 22230954
Date:
01-Nov-11     Release date:   11-Jan-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O15379  (HDAC3_HUMAN) -  Histone deacetylase 3
Seq:
Struc:
428 a.a.
369 a.a.
Protein chains
Pfam   ArchSchema ?
Q9Y618  (NCOR2_HUMAN) -  Nuclear receptor corepressor 2
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2525 a.a.
69 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.3.5.1.98  - Histone deacetylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     histone deacetylation   1 term 
  Biochemical function     chromatin binding     3 terms  

 

 
Nature 481:335-340 (2012)
PubMed id: 22230954  
 
 
Structure of HDAC3 bound to co-repressor and inositol tetraphosphate.
P.J.Watson, L.Fairall, G.M.Santos, J.W.Schwabe.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23292142 S.H.You, H.W.Lim, Z.Sun, M.Broache, K.J.Won, and M.A.Lazar (2013).
Nuclear receptor co-repressors are required for the histone-deacetylase activity of HDAC3 in vivo.
  Nat Struct Mol Biol, 20, 182-187.  
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