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The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome
 
 
DOI:10.2210/pdb1l1y/pdb
1L1Y
 
Primary Citation
spinning wheel
 
 
  •  
    Move Section Molecular Description Hide
    Classification: Hydrolase
    Structure Weight: 461887.17
     
    Molecule:cellobiohydrolase
    Polymer:1Type:polypeptide(L)Length:678
    Chains:A, B, C, D, E, F
    EC#:3.2.1.4 Go to IUBMB EC entry  
     
     
  •  
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    Polymer: 1
    Scientific Name: Clostridium thermocellum Go to NCBI Taxonomy entry Expression System: Escherichia coli  
    Polymer: 2
    Scientific Name: Synthetic construct Go to NCBI Taxonomy entry  
     
     
  •  
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    Id Details
    1L2A  The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum cellulosome 
     
     
  •  
    Move Section Ligand Chemical Component Hide
    Identifier Name Formula Interaction View Links
    BGC     BETA-D-GLUCOSE C6 H12 O6 3DLigand Explorer Link out to Ligand Expos:BGC Link out to SuperLigands:BGC Link out to SuperHapten:BGC
     
     
  •  
    Move Section Derived Data Hide
     
     
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< Biological Assembly 1    Help >
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Biological assembly 1 assigned by authors
 
 
 
  •  
    Move Section Deposition Summary Hide
    Authors:   Guimaraes, B.G.,   Souchon, H.,   Lytle, B.L.,   Wu, J.H.D.,   Alzari, P.M.

    Deposition:   2002-02-20
    Release:   2002-07-17
    Last Modified (REVDAT):   2009-02-24
     
     
  •  
    Move Section Experimental Details Hide
    Method:   X-RAY DIFFRACTION
    Experimental Data:   Download Structure Factors  [ EDS External Link to EDS ]
    View a histogram of Resolution Resolution[Å]: 2.40
    R-Value: 0.191 (obs.)
    R-Free: 0.224
    Space Group: P 21 21 21
    Unit Cell:
      Length [Å] Angles [°]
    a = 147.24 α = 90.00 
    b = 207.20 β = 90.00 
    c = 213.22 γ = 90.00