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Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Eschericia coli.
 
 
DOI:10.2210/pdb1s5p/pdb
1S5P
 
Primary Citation
spinning wheel
 
 
  •  
    Move Section Molecular Description Hide
    Classification: Hydrolase
    Structure Weight: 27109.31
     
    Molecule:NAD-dependent deacetylase
    Polymer:1Type:polypeptide(L)Length:235
    Chains:A
    EC#:3.5.1.- Go to IUBMB EC entry  
    Molecule:HISTONE H4 (RESIDUES 12-19)
    Polymer:2Type:polypeptide(L)Length:8
    Chains:B
     
     
  •  
    Move Section Source Hide
    Polymer: 1
    Scientific Name: Escherichia coli Go to NCBI Taxonomy entry Expression System: Escherichia coli bl21(de3)  
    Polymer: 2
    Scientific Name: Synthetic construct Go to NCBI Taxonomy entry  
     
     
  •  
    Move Section Ligand Chemical Component Hide
    Identifier Name Formula Interaction View Links
    ZN     ZINC ION Zn 3DLigand Explorer Link out to Ligand Expos:ZN Link out to SuperLigands:ZN Link out to SuperHapten:ZN
     
     
  •  
    Move Section Modified Residues Hide
    Identifier Name Formula Interaction View Links
    ALY N(6)-ACETYLLYSINE (parent: LYS)(type: lPeptideLinking) C8 H16 N2 O3 3D Ligand Explorer Link out to Ligand Expos:ALY Link out to SuperLigands:ALY Link out to SuperHapten:ALY 2D
     
     
  •  
    Move Section Derived Data Hide
     
     
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Biological assembly assigned by authors and generated by PISA (software)
 
 
 
  •  
    Move Section Deposition Summary Hide
    Authors:   Zhao, K.,   Chai, X.,   Marmorstein, R.

    Deposition:   2004-01-21
    Release:   2004-03-23
    Last Modified (REVDAT):   2009-02-24
     
     
  •  
    Move Section Experimental Details Hide
    Method:   X-RAY DIFFRACTION
    Experimental Data:   Download Structure Factors
    View a histogram of Resolution Resolution[Å]: 1.96
    R-Value: 0.234 (obs.)
    R-Free: 0.270
    Space Group: P 41 21 2
    Unit Cell:
      Length [Å] Angles [°]
    a = 93.91 α = 90.00 
    b = 93.91 β = 90.00 
    c = 61.49 γ = 90.00