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3FR9

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 Residues14
DetailsBINDING SITE FOR RESIDUE GSH A 212
ChainResidue
APHE10
AHOH238
AHOH244
AHOH263
BPHE42
BASP105
APHE45
AGLU57
AGLN58
AVAL59
AGLN71
ASER72
AHOH222
AHOH228

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 213
ChainResidue
AASN111
ALEU115

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GSH B 212
ChainResidue
APHE42
AASP105
BPHE10
BPHE45
BGLU57
BGLN58
BVAL59
BPRO60
BGLN71
BSER72
BHOH232
BHOH256

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 213
ChainResidue
BASN111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsDomain: {"description":"GST N-terminal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
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

239492

PDB entries from 2025-07-30

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