4GST

REACTION COORDINATE MOTION IN AN SNAR REACTION CATALYZED BY GLUTATHIONE TRANSFERASE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Observed: 0.180 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase.

Ji, X.Armstrong, R.N.Gilliland, G.L.

(1993) Biochemistry 32: 12949-12954

  • DOI: https://doi.org/10.1021/bi00211a001
  • Primary Citation of Related Structures:  
    4GST, 5GST

  • PubMed Abstract: 

    The three-dimensional structures of a class mu glutathione transferase in complex with a transition-state analogue, 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate, and a product, 1-(S-glutathionyl)-2,4-dinitrobenzene, of a nucleophilic aromatic substitution (SNAr) reaction have been determined at 1.9- and 2.0-A resolution, respectively. The two structures represent snapshots along the reaction coordinate for the enzyme-catalyzed reaction of glutathione with 1-chloro-2,4-dinitrobenzene and reveal specific interactions between the enzyme, intermediate, and product that are important in catalysis. The geometries of the intermediate and product are used to postulate reaction coordinate motion during catalysis.


  • Organizational Affiliation

    Department of Chemistry and Biochemistry, University of Maryland, College Park 20742.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GLUTATHIONE S-TRANSFERASE
A, B
217Rattus rattusMutation(s): 0 
EC: 2.5.1.18
UniProt
Find proteins for P04905 (Rattus norvegicus)
Explore P04905 
Go to UniProtKB:  P04905
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04905
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Observed: 0.180 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 88.24α = 90
b = 69.44β = 106.01
c = 81.28γ = 90
Software Package:
Software NamePurpose
GPRLSArefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1993-10-31
    Type: Initial release
  • Version 1.1: 2008-03-25
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-11-29
    Changes: Derived calculations, Other
  • Version 1.4: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Structure summary