2J13

Structure of a family 4 carbohydrate esterase from Bacillus anthracis

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.188 

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This is version 1.3 of the entry. See complete history. 


Literature

Structure of a Carbohydrate Esterase from Bacillus Anthracis.

Oberbarnscheidt, L., Taylor, E.J., Davies, G.J., Gloster, T.M.

(2007) Proteins 66: 250


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
POLYSACCHARIDE DEACETYLASE247Bacillus anthracis str. AmesMutation(s): 0 
EC: 3.5.1
UniProt
Find proteins for A0A6H3ACS3 (Bacillus anthracis)
Explore A0A6H3ACS3 
Go to UniProtKB:  A0A6H3ACS3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A6H3ACS3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.188 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 56.927α = 90
b = 56.927β = 90
c = 158.531γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-10-03
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description