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PDBsum entry 3fr3

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3fr3
Jmol
Contents
Protein chains
201 a.a. *
Ligands
GDS ×2
Waters ×212
* Residue conservation analysis
PDB id:
3fr3
Name: Transferase
Title: Tetramerization and cooperativity in plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Structure: Glutathione s-transferase. Chain: a, b. Synonym: pfgst. Engineered: yes. Mutation: yes
Source: Plasmodium falciparum. Organism_taxid: 5833. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.213     R-free:   0.252
Authors: M.Perbandt,E.Liebau,G.Ricci
Key ref: M.Perbandt et al. Tetramerization and cooperativity in plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118. To be published, .
Date:
08-Jan-09     Release date:   26-Jan-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8MU52  (GST_PLAFA) -  Glutathione S-transferase
Seq:
Struc:
211 a.a.
201 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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
Bound ligand (Het Group name = GDS)
matches with 50.00% similarity
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site