1BX9

GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH HERBICIDE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.196 

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This is version 1.2 of the entry. See complete history. 


Literature

Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase - explanations for the selectivity of the enzyme in plants.

Prade, L., Huber, R., Bieseler, B.

(1998) Structure 6: 1445-1452

  • DOI: https://doi.org/10.1016/s0969-2126(98)00143-9
  • Primary Citation of Related Structures:  
    1BX9, 1BYE

  • PubMed Abstract: 

    Glutathione S-transferases (GSTs) are detoxifying enzymes present in all aerobic organisms. These enzymes catalyse the conjugation of glutathione with a variety of electrophilic compounds. In plants, GSTs catalyse the first step in the degradation of several herbicides, such as triazines and acetamides, thus playing an important role in herbicide tolerance.

    • Organizational Affiliation: 

    Max Planck Institut für Biochemie Abt. Strukturforschung Am Klopferspitz 18a D-82152 Martinsrie, Germany. lars.prade@pharma.novartis.com


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GLUTATHIONE S-TRANSFERASE211Arabidopsis thalianaMutation(s): 0 
UniProt
Find proteins for P46422 (Arabidopsis thaliana)
Explore P46422 
Go to UniProtKB:  P46422
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP46422
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
FOE-4053-glutathione conjugate GGL-FOE-GLY3N/AMutation(s): 0 
Sequence Annotations
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  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
FOE
Query on FOE
B
L-PEPTIDE LINKINGC14 H19 F N2 O3 SCYS
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.196 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59α = 90
b = 88.83β = 90
c = 89.85γ = 90
Software Package:
Software NamePurpose
X-PLORrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-10-21
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Database references, Derived calculations, Non-polymer description, Version format compliance