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2GSR

Structure of porcine class pi glutathione s-transferase

Replaces:  1GSR
Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0006749biological_processglutathione metabolic process
A0016740molecular_functiontransferase activity
A0051122biological_processhepoxilin biosynthetic process
A0110076biological_processnegative regulation of ferroptosis
A1901687biological_processglutathione derivative biosynthetic process
B0004364molecular_functionglutathione transferase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006693biological_processprostaglandin metabolic process
B0006749biological_processglutathione metabolic process
B0016740molecular_functiontransferase activity
B0051122biological_processhepoxilin biosynthetic process
B0110076biological_processnegative regulation of ferroptosis
B1901687biological_processglutathione derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GTS A 208
ChainResidue
ATYR7
ASER63
AHOH227
AHOH271
AHOH334
AHOH336
AHOH338
BMET35
BGLU36
BASP96
APHE8
AARG13
ATRP38
ALYS42
AGLN49
ALEU50
APRO51
AGLN62

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GTS B 208
ChainResidue
AASP96
BTYR7
BPHE8
BARG13
BTRP38
BLYS42
BGLN49
BLEU50
BPRO51
BGLN62
BSER63
BHOH217
BHOH235
BHOH273
BHOH326
BHOH327
BHOH328
BHOH330

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues154
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues242
DetailsDomain: {"description":"GST C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7932743","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by EGFR","evidences":[{"source":"UniProtKB","id":"P09211","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P09211","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P19157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P09211","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR7

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR7

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PDB entries from 2025-12-17

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