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1A0F

CRYSTAL STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM ESCHERICHIA COLI COMPLEXED WITH GLUTATHIONESULFONIC ACID

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005737cellular_componentcytoplasm
A0016740molecular_functiontransferase activity
A0042542biological_processresponse to hydrogen peroxide
A0042803molecular_functionprotein homodimerization activity
B0004364molecular_functionglutathione transferase activity
B0005737cellular_componentcytoplasm
B0016740molecular_functiontransferase activity
B0042542biological_processresponse to hydrogen peroxide
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GTS A 203
ChainResidue
AALA9
ALYS107
AHOH246
AHOH247
BASN99
BTHR103
BGLU104
ACYS10
ALEU32
ALYS35
AGLN51
AVAL52
AGLU65
AGLY66
AHIS106

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GTS B 203
ChainResidue
AASN99
ATHR103
AGLU104
BALA9
BCYS10
BLEU32
BLYS35
BGLN51
BVAL52
BGLU65
BGLY66
BHIS106
BLYS107
BTRP164
BHOH234
BHOH235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:9680481
ChainResidueDetails
ACYS10
BGLU65
BASN99
BTHR103
ALYS35
AVAL52
AGLU65
AASN99
ATHR103
BCYS10
BLYS35
BVAL52

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR5

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR5

237735

PDB entries from 2025-06-18

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