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Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD+-dependent Sir2 histone/protein deacetylases
1SZD
Primary Citation
 
 
  •   Molecular Description Hide
    Classification: Gene Regulation
    Structure Weight: 35610.60
    Molecule: NAD-dependent deacetylase HST2
    Polymer: 1 Type: protein Length: 297
    Chains: A
    EC#: 3.5.1   
    Fragment: catalytic core domain
    Organism: Saccharomyces cerevisiae
    Gene Names: HST2 YPL015C LPA2C
    UniProtKB: Protein Feature View | Search PDB | P53686  
    Molecule: Histone H4 peptide
    Polymer: 2 Type: protein Length: 10
    Chains: B
    Organism: Saccharomyces cerevisiae S288c
    Gene Names: HHF1 YBR009C YBR0122 HHF2 YNL030W N2752
    UniProtKB: Protein Feature View | Search PDB | P02309  
     
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  •   Source Hide
    Polymer: 1
    Scientific Name: Saccharomyces cerevisiae   Taxonomy   Common Name: Baker's yeast Expression System: Escherichia coli  
    Polymer: 2
    Scientific Name: Synthetic construct (Saccharomyces cerevisiae S288c)   Taxonomy    
     
  •   Related PDB Entries Hide
    Identifier Details
    1Q14  Structure and Autoregulation Of The Yeast Hst2 Homolog Of Sir2 
    1Q17  Structure Of The Yeast Hst2 Protein Deacetylase In Ternary Complex With 2'-O-Acetyl ADP Ribose and Histone Peptide 
    1Q1A  Structure Of The Yeast Hst2 Protein Deacetylase In Ternary Complex With 2'-O-Acetyl ADP Ribose and Histone Peptide 
    1SZC  Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD+-dependent Sir2 histone/protein deacetylases 
     
  •   Ligand Chemical Component Hide
     
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    Identifier   Binding Affinity (Sequence Identity %)
    APR
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    APR
    N/Ain BindingDB
    Kd: 29160 nM - data from BindingMOAD  
    N/Ain PDBbind
     
  •   Modified Residues Hide
    Identifier Formula Parent Type
    ALY
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    ALY C8 H16 N2 O3 LYS lPeptideLinking
     
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  •   Structural Biology Knowledgebase Data Hide
     
 
Data in orange boxes are gathered from external resources (when available).
 
  Biological Assembly 1       
Biological assembly 1 assigned by authors and generated by PISA (software)
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  •   Deposition Summary Hide
    Authors:   Zhao, K.,  Harshaw, R.,  Chai, X.,  Marmorstein, R.

    Deposition:   2004-04-05
    Release:   2004-06-15
    Last Modified (REVDAT):   2011-07-13
     
  •   Revision History    Hide
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    2011-07-13
    Version format compliance
    2011-07-13
    Non-polymer description
     
  •   Experimental Details Hide
    Method:   X-RAY DIFFRACTION
    Exp. Data:
      Structure Factors
    EDS  
    Resolution[Å]:   1.50
    R-Value: 0.214 (obs.)
    R-Free: 0.230
    Space Group: P 32 2 1
    Unit Cell:
      Length [Å] Angles [°]
    a = 105.38 α = 90.00 
    b = 105.38 β = 90.00 
    c = 66.15 γ = 120.00