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1Q4J

Crystal Structure of Pf-GST1 with its inhibitor s-hexyl-GSH

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 Residues17
DetailsBINDING SITE FOR RESIDUE GTX A 212
ChainResidue
ATYR9
AASN111
AHOH216
AHOH242
AHOH249
BPHE116
BLYS117
BGLU120
BTHR121
ALYS15
APHE45
AGLN58
AVAL59
APRO60
AGLN71
ASER72
AASP105

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GTX B 212
ChainResidue
APHE116
ALYS117
AGLU120
ATHR121
AHOH268
BTYR9
BLYS15
BPHE45
BGLN58
BVAL59
BPRO60
BGLN71
BSER72
BASP105
BASN111
BHOH218
BHOH225
BHOH252

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 Residues244
DetailsDomain: {"description":"GST C-terminal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12972411","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3FR9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR9

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR9

239803

PDB entries from 2025-08-06

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