PDBsum entry 3vwx

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Transferase PDB id
Protein chains
218 a.a.
GSH ×4
Waters ×934
PDB id:
Name: Transferase
Title: Structural analysis of an epsilon-class glutathione s-transf housefly, musca domestica
Structure: Glutathione s-transferase 6b. Chain: a, b, c, d. Engineered: yes. Mutation: yes
Source: Musca domestica. House fly. Organism_taxid: 7370. Gene: gst-6b. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.80Å     R-factor:   0.165     R-free:   0.191
Authors: C.Nakamura,M.Sue,T.Miyamoto,S.Yajima
Key ref: C.Nakamura et al. (2013). Structural analysis of an epsilon-class glutathione transferase from housefly, Musca domestica. Biochem Biophys Res Commun, 430, 1206-1211. PubMed id: 23268341 DOI: 10.1016/j.bbrc.2012.12.077
05-Sep-12     Release date:   27-Feb-13    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q9U795  (Q9U795_MUSDO) -  Glutathione s-transferase 6B
222 a.a.
218 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
Bound ligand (Het Group name = GSH)
corresponds exactly
= 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  


DOI no: 10.1016/j.bbrc.2012.12.077 Biochem Biophys Res Commun 430:1206-1211 (2013)
PubMed id: 23268341  
Structural analysis of an epsilon-class glutathione transferase from housefly, Musca domestica.
C.Nakamura, S.Yajima, T.Miyamoto, M.Sue.
Glutathione transferases (GSTs) play an important role in the detoxification of insecticides, and as such, they are a key contributor to enhanced resistance to insecticides. In the housefly (Musca domestica), two epsilon-class GSTs (MdGST6A and MdGST6B) that share high sequence homology have been identified, which are believed to be involved in resistance against insecticides. The structural determinants controlling the substrate specificity and enzyme activity of MdGST6s are unknown. The aim of this study was to crystallize and perform structural analysis of the GST isozyme, MdGST6B. The crystal structure of MdGST6B complexed with reduced glutathione (GSH) was determined at a resolution of 1.8Å. MdGST6B was found to have a typical GST folding comprised of N-terminal and C-terminal domains. Arg113 and Phe121 on helix 4 were shown to protrude into the substrate binding pocket, and as a result, the entrance of the substrate binding pocket was narrower compared to delta- and epsilon-class GSTs from Africa malaria vector Anopheles gambiae, agGSTd1-6 and agGSTe2, respectively. This substrate pocket narrowing is partly due to the presence of a π-helix in the middle of helix 4. Among the six residues that donate hydrogen bonds to GSH, only Arg113 was located in the C-terminal domain. Ala substitution of Arg113 did not have a significant effect on enzyme activity, suggesting that the Arg113 hydrogen bond does not play a crucial role in catalysis. On the other hand, mutation at Phe108, located just below Arg113 in the binding pocket, reduced the affinity and catalytic activity to both GSH and the electrophilic co-substrate, 1-chloro-2,4-dinitrobenzene.