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3FR6

Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0006749biological_processglutathione metabolic process
A0016740molecular_functiontransferase activity
B0004364molecular_functionglutathione transferase activity
B0006749biological_processglutathione metabolic process
B0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 212
ChainResidue
AGLN71
ASER72
AGLN73

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 212
ChainResidue
BLYS15
BSER72
BGLN73

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues168
DetailsDomain: {"description":"GST N-terminal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12972411","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3FR9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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