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PDBsum entry 3rqd

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protein ligands metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
3rqd
Jmol
Contents
Protein chains
354 a.a.
Ligands
02G-GLY-BB9-03Y-
VAL
×2
Metals
__K ×4
_ZN ×2
Waters ×504
PDB id:
3rqd
Name: Hydrolase/hydrolase inhibitor
Title: Ideal thiolate-zinc coordination geometry in depsipeptide bi histone deacetylase 8
Structure: Histone deacetylase 8. Chain: a, b. Synonym: hd8. Engineered: yes. Largazole. Chain: c, d. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hdac8, hdacl1, cda07. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Symploca. Organism_taxid: 105591
Resolution:
2.14Å     R-factor:   0.204     R-free:   0.245
Authors: K.E Cole,D.P.Dowling,D.W.Christianson
Key ref: K.E.Cole et al. (2011). Structural basis of the antiproliferative activity of largazole, a depsipeptide inhibitor of the histone deacetylases. J Am Chem Soc, 133, 12474-12477. PubMed id: 21790156 DOI: 10.1021/ja205972n
Date:
28-Apr-11     Release date:   24-Aug-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9BY41  (HDAC8_HUMAN) -  Histone deacetylase 8
Seq:
Struc:
377 a.a.
354 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.5.1.98  - Histone deacetylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     plasma membrane   6 terms 
  Biological process     mitotic cell cycle   12 terms 
  Biochemical function     hydrolase activity     11 terms  

 

 
DOI no: 10.1021/ja205972n J Am Chem Soc 133:12474-12477 (2011)
PubMed id: 21790156  
 
 
Structural basis of the antiproliferative activity of largazole, a depsipeptide inhibitor of the histone deacetylases.
K.E.Cole, D.P.Dowling, M.A.Boone, A.J.Phillips, D.W.Christianson.
 
  ABSTRACT  
 
No abstract given.