Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1GTU

LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M1A-1A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0006749biological_processglutathione metabolic process
A0016740molecular_functiontransferase activity
A0018916biological_processnitrobenzene metabolic process
A0019899molecular_functionenzyme binding
A0042178biological_processxenobiotic catabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043295molecular_functionglutathione binding
A0051122biological_processhepoxilin biosynthetic process
A0070458biological_processcellular detoxification of nitrogen compound
A1901687biological_processglutathione derivative biosynthetic process
B0004364molecular_functionglutathione transferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006693biological_processprostaglandin metabolic process
B0006749biological_processglutathione metabolic process
B0016740molecular_functiontransferase activity
B0018916biological_processnitrobenzene metabolic process
B0019899molecular_functionenzyme binding
B0042178biological_processxenobiotic catabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043295molecular_functionglutathione binding
B0051122biological_processhepoxilin biosynthetic process
B0070458biological_processcellular detoxification of nitrogen compound
B1901687biological_processglutathione derivative biosynthetic process
C0004364molecular_functionglutathione transferase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006629biological_processlipid metabolic process
C0006693biological_processprostaglandin metabolic process
C0006749biological_processglutathione metabolic process
C0016740molecular_functiontransferase activity
C0018916biological_processnitrobenzene metabolic process
C0019899molecular_functionenzyme binding
C0042178biological_processxenobiotic catabolic process
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0043295molecular_functionglutathione binding
C0051122biological_processhepoxilin biosynthetic process
C0070458biological_processcellular detoxification of nitrogen compound
C1901687biological_processglutathione derivative biosynthetic process
D0004364molecular_functionglutathione transferase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006629biological_processlipid metabolic process
D0006693biological_processprostaglandin metabolic process
D0006749biological_processglutathione metabolic process
D0016740molecular_functiontransferase activity
D0018916biological_processnitrobenzene metabolic process
D0019899molecular_functionenzyme binding
D0042178biological_processxenobiotic catabolic process
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0043295molecular_functionglutathione binding
D0051122biological_processhepoxilin biosynthetic process
D0070458biological_processcellular detoxification of nitrogen compound
D1901687biological_processglutathione derivative biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues344
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues472
DetailsDomain: {"description":"GST C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2005","submissionDatabase":"PDB data bank","title":"Human glutathione S-transferase M1A-1A catalyzes formation of Gsh-metal complexes.","authors":["Patskovsky Y.V.","Patskovska L.N.","Listowsky I.","Almo S.C."]}},{"source":"PubMed","id":"16548513","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10649","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04905","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR6

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR6

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
CTYR6

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
DTYR6

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon