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PDBsum entry 1y6e

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protein Protein-protein interface(s) links
Transferase PDB id
1y6e
Jmol
Contents
Protein chains
216 a.a. *
Waters ×16
* Residue conservation analysis
PDB id:
1y6e
Name: Transferase
Title: Orthorhombic glutathione s-transferase of schistosoma japonicum
Structure: Glutathione s-transferase. Chain: a, b. Engineered: yes
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Biol. unit: Dimer (from PQS)
Resolution:
3.00Å     R-factor:   0.211     R-free:   0.279
Authors: A.C.Rufer,L.Thiebach,K.Baer,H.W.Klein,M.Hennig
Key ref:
A.C.Rufer et al. (2005). X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site. Acta Crystallograph Sect F Struct Biol Cryst Commun, 61, 263-265. PubMed id: 16511012 DOI: 10.1107/S1744309105004823
Date:
06-Dec-04     Release date:   08-Mar-05    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08515  (GST26_SCHJA) -  Glutathione S-transferase class-mu 26 kDa isozyme
Seq:
Struc:
218 a.a.
216 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.5.1.18  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
RX
+ glutathione
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S1744309105004823 Acta Crystallograph Sect F Struct Biol Cryst Commun 61:263-265 (2005)
PubMed id: 16511012  
 
 
X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site.
A.C.Rufer, L.Thiebach, K.Baer, H.W.Klein, M.Hennig.
 
  ABSTRACT  
 
The crystal structure of the 26 kDa glutathione S-transferase from Schistosoma japonicum (SjGST) was determined at 3 A resolution in the new space group P2(1)2(1)2(1). The structure of orthorhombic SjGST reveals unique features of the ligand-binding site and dimer interface when compared with previously reported structures. SjGST is recognized as the major detoxification enzyme of S. japonicum, a pathogenic helminth causing schistosomiasis. As resistance against the established inhibitor of SjGST, praziquantel, has been reported these results might prove to be valuable for the development of novel drugs.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 Stereoview of the reciprocal dimer contact between Tyr103 and Arg107 of chains A (blue) and B (magenta). The distance of the hydroxy O atom of Tyr103A to the terminal amino N atom of Arg107B is 3.3 Å and N^ of Arg107A is 3.5 Å away from the hydroxy O atom of Tyr103B. Residues Arg107 of chains A and B each hydrogen bond (3.3 and 3.1 Å distance to W16 and W15, respectively) to water molecules.
 
  The above figure is reprinted from an Open Access publication published by the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2005, 61, 263-265) copyright 2005.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18499670 E.Mantuano, G.Mukandala, X.Li, W.M.Campana, and S.L.Gonias (2008).
Molecular dissection of the human alpha2-macroglobulin subunit reveals domains with antagonistic activities in cell signaling.
  J Biol Chem, 283, 19904-19911.  
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