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1EEM

GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006749biological_processglutathione metabolic process
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A0014810biological_processpositive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0019852biological_processL-ascorbic acid metabolic process
A0042178biological_processxenobiotic catabolic process
A0045174molecular_functionglutathione dehydrogenase (ascorbate) activity
A0050610molecular_functionmethylarsonate reductase activity
A0051280biological_processnegative regulation of release of sequestered calcium ion into cytosol
A0051281biological_processpositive regulation of release of sequestered calcium ion into cytosol
A0070062cellular_componentextracellular exosome
A0071243biological_processcellular response to arsenic-containing substance
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
AARG39
AHIS49
AVAL51
AHOH1009

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 902
ChainResidue
AHOH1137
AGLU21
AGLY22
ASER78
AGLN79
AHOH1021

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GSH A 999
ChainResidue
ACYS32
APHE34
ALEU56
ALYS59
ALEU71
AVAL72
APRO73
AGLU85
ASER86
AHOH1002
AHOH1030
AHOH1043

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues79
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues124
DetailsDomain: {"description":"GST C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10783391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10783391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21106529","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ASER28

246333

PDB entries from 2025-12-17

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