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Structure paper

TitleTetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Journal, issue, pagesTo be Published
Publish dateJan 8, 2009 (structure data deposition date)
AuthorsPerbandt, M. / Liebau, E. / Ricci, G.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.9 - 2.6 Å
Structure data

PDB-3fr3:
Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3fr6:
Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3fr9:
Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3frc:
Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-GDS:
OXIDIZED GLUTATHIONE DISULFIDE

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-GSH:
GLUTATHIONE

ChemComp-CL:
Unknown entry

ChemComp-0HG:
N-[(4S)-4-ammonio-4-carboxybutanoyl]-S-(4-bromobenzyl)-L-cysteinylglycine

Source
  • plasmodium falciparum (malaria parasite P. falciparum)
KeywordsTRANSFERASE / plasmodium falciparum / pfgst / oxidative stress / Glutathione S-transferase / PfGST1

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