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PDBsum entry 3mak

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protein ligands links
Transferase PDB id
3mak
Jmol
Contents
Protein chain
208 a.a.
Ligands
GSH
Waters ×212
PDB id:
3mak
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.
Resolution:
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. Structure of a drosophila delta class glutathione transferase. To be published, .
Date:
24-Mar-10     Release date:   30-Mar-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P20432  (GSTT1_DROME) -  Glutathione S-transferase 1-1
Seq:
Struc:
209 a.a.
208 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: E.C.2.5.1.18  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
RX
+
glutathione
Bound ligand (Het Group name = GSH)
corresponds exactly
= HX
+ R-S-glutathione
   Enzyme class 3: E.C.4.5.1.1  - 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
1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane
= 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!
  Biological process     glutathione metabolic process   1 term 
  Biochemical function     transferase activity     4 terms