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1GSE

GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004601molecular_functionperoxidase activity
A0004602molecular_functionglutathione peroxidase activity
A0004769molecular_functionsteroid Delta-isomerase activity
A0005504molecular_functionfatty acid binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0006749biological_processglutathione metabolic process
A0006805biological_processxenobiotic metabolic process
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0016853molecular_functionisomerase activity
A0030855biological_processepithelial cell differentiation
A0042167biological_processheme catabolic process
A0043651biological_processlinoleic acid metabolic process
A0070062cellular_componentextracellular exosome
A0098869biological_processcellular oxidant detoxification
A0140104molecular_functionmolecular carrier activity
A1901687biological_processglutathione derivative biosynthetic process
B0004364molecular_functionglutathione transferase activity
B0004601molecular_functionperoxidase activity
B0004602molecular_functionglutathione peroxidase activity
B0004769molecular_functionsteroid Delta-isomerase activity
B0005504molecular_functionfatty acid binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006693biological_processprostaglandin metabolic process
B0006749biological_processglutathione metabolic process
B0006805biological_processxenobiotic metabolic process
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0016853molecular_functionisomerase activity
B0030855biological_processepithelial cell differentiation
B0042167biological_processheme catabolic process
B0043651biological_processlinoleic acid metabolic process
B0070062cellular_componentextracellular exosome
B0098869biological_processcellular oxidant detoxification
B0140104molecular_functionmolecular carrier activity
B1901687biological_processglutathione derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GSH A 223
ChainResidue
ATYR9
AHOH297
AHOH406
BASP101
BARG131
BHOH285
AARG45
AGLN54
AVAL55
APRO56
AGLN67
ATHR68
AEAA224
AHOH236

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE EAA A 224
ChainResidue
ATYR9
APHE10
AARG13
AGLY14
ALYS15
ALEU107
ALEU108
AVAL111
AMET208
AALA216
APHE220
APHE222
AGSH223
AHOH312

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 225
ChainResidue
ASER18
AILE96
ABME226
AHOH378

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BME A 226
ChainResidue
AARG69
ALEU72
AILE96
AGLU97
AHIS159
ABME225
AHOH227
AHOH289
AHOH379

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GSH B 223
ChainResidue
AASP101
AARG131
AHOH284
BTYR9
BARG45
BGLN54
BVAL55
BPRO56
BGLN67
BTHR68
BEAA224
BHOH242
BHOH300
BHOH301
BHOH320

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE EAA B 224
ChainResidue
BTYR9
BPHE10
BARG13
BGLY14
BLYS15
BLEU107
BLEU108
BPRO110
BVAL111
BMET208
BALA216
BPHE220
BGSH223
BHOH241
BHOH316

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME B 225
ChainResidue
BSER18
BILE96
BBME226
BHOH344

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BME B 226
ChainResidue
BARG69
BILE96
BGLU97
BHIS159
BBME225
BHOH233
BHOH291

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues160
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues244
DetailsDomain: {"description":"GST C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16421451","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19618965","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed","evidences":[{"source":"UniProtKB","id":"P30115","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P30115","evidenceCode":"ECO:0000250"}]}
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

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PDB entries from 2025-12-03

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