PDBsum entry 3mak

Go to PDB code: 
protein ligands links
Transferase PDB id
Jmol PyMol
Protein chain
208 a.a.
Waters ×212
PDB id:
Name: Transferase
Title: Crystal structure of glutathione transferase dmgstd1 from dr melanogaster, in complex with glutathione
Structure: Glutathione s-transferase 1-1. Chain: a. Synonym: glutathione transferase dmgstd1, gst class-theta. Engineered: yes
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: gstd1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
1.80Å     R-factor:   0.162     R-free:   0.200
Authors: J.Wongsantichon,R.C.Robinson,A.J.Ketterman
Key ref: J.Wongsantichon et al. (2012). Structural evidence for conformational changes of Delta class glutathione transferases after ligand binding. Arch Biochem Biophys, 521, 77-83. PubMed id: 22475449
24-Mar-10     Release date:   30-Mar-11    
Go to PROCHECK summary

Protein chain
-  (POLG_HAVHM) - 
Protein chain
Pfam   ArchSchema ?
P20432  (GSTT1_DROME) -  Glutathione S-transferase D1
209 a.a.
208 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: 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
   Enzyme class 3: E.C.  - DDT-dehydrochlorinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2- bis(4-chlorophenyl)ethylene + chloride
= 1,1-dichloro-2,2- bis(4-chlorophenyl)ethylene
+ chloride
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     response to toxin   2 terms 
  Biochemical function     transferase activity     4 terms  


Arch Biochem Biophys 521:77-83 (2012)
PubMed id: 22475449  
Structural evidence for conformational changes of Delta class glutathione transferases after ligand binding.
J.Wongsantichon, R.C.Robinson, A.J.Ketterman.
We report four new crystal structures for Delta class glutathione transferases from insects. We compare these new structures as well as several previously reported structures to determine that structural transitions can be observed with ligand binding. These transitions occurred in the regions around the active site entrance, including alpha helix 2, C-terminus of alpha helix 4 including the loop to helix 5 and the C-terminus of helix 8. These structural movements have been reported or postulated to occur for several other glutathione transferase classes; however, this is the first report showing structural evidence of all these movements occurring, in this case in Delta class glutathione transferases. These fluctuations also can be observed occurring within a single structure as there is ligand bound in only one subunit and each subunit is undergoing different conformational transitions. The structural comparisons show reorganizations occur both pre- and post-GSH ligand binding communicated through the subunit interface of the quaternary assembly. Movements of these positions would allow 'breathing' of the active site for substrate entrance, topological rearrangement for varying substrate specificity and final product release.