3NDZ

The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.08 Å
  • R-Value Free: 0.193 
  • R-Value Work: 0.144 
  • R-Value Observed: 0.146 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history


Literature

The structure of the catalytic and carbohydrate binding domain of endoglucanase D bound to cellotriose

Bianchetti, C.M.Smith, R.W.Bingman, C.A.Phillips Jr., G.N.

To be published.

Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Endoglucanase DA,
C [auth B],
E [auth C],
G [auth D]
345Clostridium cellulovoransMutation(s): 0 
Gene Names: engD
EC: 3.2.1.4
UniProt
Find proteins for P28623 (Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B))
Explore P28623 
Go to UniProtKB:  P28623
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP28623
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Endoglucanase DB [auth E],
D [auth F],
F [auth G],
H
107Clostridium cellulovoransMutation(s): 0 
Gene Names: engD
EC: 3.2.1.4
UniProt
Find proteins for P28623 (Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B))
Explore P28623 
Go to UniProtKB:  P28623
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP28623
Sequence Annotations
Expand
  • Reference Sequence
Oligosaccharides

Help

Entity ID: 3
MoleculeChains Length2D Diagram Glycosylation3D Interactions
beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose
I, J, K, L, M
I, J, K, L, M, N
3N/A
Glycosylation Resources
GlyTouCan:  G14338VK
GlyCosmos:  G14338VK
GlyGen:  G14338VK
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.08 Å
  • R-Value Free: 0.193 
  • R-Value Work: 0.144 
  • R-Value Observed: 0.146 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 85.297α = 90
b = 119.05β = 90
c = 198.487γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
PHENIXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-06-29
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Atomic model, Data collection, Derived calculations, Non-polymer description, Structure summary
  • Version 2.1: 2024-02-21
    Changes: Data collection, Database references, Structure summary