Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1XW6

1.9 angstrom resolution structure of human glutathione S-transferase M1A-1A complexed with glutathione

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 PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GSH A 750
ChainResidue
ATYR6
ASER72
AMET104
AHOH764
AHOH790
AHOH807
AHOH822
AHOH886
AHOH938
BASP105
ATRP7
ALEU12
AARG42
ATRP45
ALYS49
AASN58
ALEU59
AGLN71
site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GSH B 751
ChainResidue
AASP105
BTYR6
BTRP7
BLEU12
BARG42
BTRP45
BLYS49
BASN58
BLEU59
BPRO60
BGLN71
BSER72
BHOH755
BHOH756
BHOH927
site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GSH C 752
ChainResidue
CTYR6
CTRP7
CARG42
CTRP45
CLYS49
CASN58
CLEU59
CGLN71
CSER72
CHOH770
CHOH771
CHOH829
CHOH834
CHOH885
CHOH887
DASP105
site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GSH D 753
ChainResidue
CASP105
DTYR6
DTRP7
DLEU12
DARG42
DTRP45
DLYS49
DASN58
DLEU59
DGLN71
DSER72
DMET104
DHOH766
DHOH767
DHOH818
DHOH872
DHOH886
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

243911

PDB entries from 2025-10-29

PDB statisticsPDBj update infoContact PDBjnumon