5W1J

Echinococcus granulosus thioredoxin glutathione reductas (egTGR)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.197 
  • R-Value Observed: 0.200 

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Ligand Structure Quality Assessment 


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Literature

The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I).

Salinas, G., Gao, W., Wang, Y., Bonilla, M., Yu, L., Novikov, A., Virginio, V.G., Ferreira, H.B., Vieites, M., Gladyshev, V.N., Gambino, D., Dai, S.

(2017) Antioxid Redox Signal 27: 1491-1504

  • DOI: https://doi.org/10.1089/ars.2016.6816
  • Primary Citation of Related Structures:  
    5W1J, 5W1L

  • PubMed Abstract: 

    New drugs are needed to treat flatworm infections that cause severe human diseases such as schistosomiasis. The unique flatworm enzyme thioredoxin glutathione reductase (TGR), structurally different from the human enzyme, is a key drug target. Structural studies of the flatworm Echinococcus granulosus TGR, free and complexed with Au I -MPO, a novel gold inhibitor, together with inhibition assays were performed.

    • Organizational Affiliation: 

    1 Worm Biology Lab, Institut Pasteur de Montevideo , Montevideo, Uruguay .


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Thioredoxin glutathione reductase
A, B
584Echinococcus granulosusMutation(s): 0 
Gene Names: TGR
UniProt
Find proteins for Q869D7 (Echinococcus granulosus)
Explore Q869D7 
Go to UniProtKB:  Q869D7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ869D7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.197 
  • R-Value Observed: 0.200 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 108.74α = 90
b = 108.74β = 90
c = 257.064γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-11-22
    Type: Initial release