1R5A

Glutathione S-transferase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.233 

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Ligand Structure Quality Assessment 


This is version 2.0 of the entry. See complete history


Literature

Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme.

Udomsinprasert, R.Pongjaroenkit, S.Wongsantichon, J.Oakley, A.J.Prapanthadara, L.A.Wilce, M.C.Ketterman, A.J.

(2005) Biochem J 388: 763-771

  • DOI: https://doi.org/10.1042/BJ20042015
  • Primary Citation of Related Structures:  
    1R5A, 1V2A

  • PubMed Abstract: 

    The insect GST (glutathione transferase) supergene family encodes a varied group of proteins belonging to at least six individual classes. Interest in insect GSTs has focused on their role in conferring insecticide resistance. Previously from the mosquito malaria vector Anopheles dirus, two genes encoding five Delta class GSTs have been characterized for structural as well as enzyme activities. We have obtained a new Delta class GST gene and isoenzyme from A. dirus, which we name adGSTD5-5. The adGSTD5-5 isoenzyme was identified and was only detectably expressed in A. dirus adult females. A putative promoter analysis suggests that this GST has an involvement in oogenesis. The enzyme displayed little activity for classical GST substrates, although it possessed the greatest activity for DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] observed for Delta GSTs. However, GST activity was inhibited or enhanced in the presence of various fatty acids, suggesting that the enzyme may be modulated by fatty acids. We obtained a crystal structure for adGSTD5-5 and compared it with other Delta GSTs, which showed that adGSTD5-5 possesses an elongated and more polar active-site topology.


  • Organizational Affiliation

    Institute of Molecular Biology and Genetics, Mahidol University, Salaya Campus, 25/25 Putthamonthol Road 4, Salaya, Nakon Pathom 73170, Thailand.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
glutathione transferase218Anopheles cracensMutation(s): 0 
Gene Names: adGST1-5
EC: 2.5.1.18
UniProt
Find proteins for Q9GQG7 (Anopheles cracens)
Explore Q9GQG7 
Go to UniProtKB:  Q9GQG7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9GQG7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.233 
  • Space Group: I 41 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 122.129α = 90
b = 122.129β = 90
c = 74.699γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
CNSrefinement

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

  • Released Date: 2003-10-28 
  • Deposition Author(s): Oakley, A.J.

Revision History  (Full details and data files)

  • Version 1.0: 2003-10-28
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2023-10-25
    Changes: Atomic model, Data collection, Database references, Derived calculations, Refinement description