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1EV4

RAT GLUTATHIONE S-TRANSFERASE A1-1: MUTANT W21F/F220Y WITH GSO3 BOUND

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004601molecular_functionperoxidase activity
A0004769molecular_functionsteroid Delta-isomerase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0006749biological_processglutathione metabolic process
A0006805biological_processxenobiotic metabolic process
A0009617biological_processresponse to bacterium
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0016853molecular_functionisomerase activity
A0030855biological_processepithelial cell differentiation
A0035634biological_processresponse to stilbenoid
A0035731molecular_functiondinitrosyl-iron complex binding
A0042178biological_processxenobiotic catabolic process
A0042803molecular_functionprotein homodimerization activity
A0043295molecular_functionglutathione binding
A0098869biological_processcellular oxidant detoxification
A1901687biological_processglutathione derivative biosynthetic process
C0004364molecular_functionglutathione transferase activity
C0004601molecular_functionperoxidase activity
C0004769molecular_functionsteroid Delta-isomerase activity
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0006629biological_processlipid metabolic process
C0006693biological_processprostaglandin metabolic process
C0006749biological_processglutathione metabolic process
C0006805biological_processxenobiotic metabolic process
C0009617biological_processresponse to bacterium
C0016491molecular_functionoxidoreductase activity
C0016740molecular_functiontransferase activity
C0016853molecular_functionisomerase activity
C0030855biological_processepithelial cell differentiation
C0035634biological_processresponse to stilbenoid
C0035731molecular_functiondinitrosyl-iron complex binding
C0042178biological_processxenobiotic catabolic process
C0042803molecular_functionprotein homodimerization activity
C0043295molecular_functionglutathione binding
C0098869biological_processcellular oxidant detoxification
C1901687biological_processglutathione derivative biosynthetic process
D0004364molecular_functionglutathione transferase activity
D0004601molecular_functionperoxidase activity
D0004769molecular_functionsteroid Delta-isomerase activity
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0006629biological_processlipid metabolic process
D0006693biological_processprostaglandin metabolic process
D0006749biological_processglutathione metabolic process
D0006805biological_processxenobiotic metabolic process
D0009617biological_processresponse to bacterium
D0016491molecular_functionoxidoreductase activity
D0016740molecular_functiontransferase activity
D0016853molecular_functionisomerase activity
D0030855biological_processepithelial cell differentiation
D0035634biological_processresponse to stilbenoid
D0035731molecular_functiondinitrosyl-iron complex binding
D0042178biological_processxenobiotic catabolic process
D0042803molecular_functionprotein homodimerization activity
D0043295molecular_functionglutathione binding
D0098869biological_processcellular oxidant detoxification
D1901687biological_processglutathione derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 260
ChainResidue
ATHR77
AASP85
AMET86
AARG89
AHOH537

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 261
ChainResidue
CASP85
CMET86
CARG89

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 262
ChainResidue
DASP85
DMET86
DARG89
CTHR77

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GTS A 230
ChainResidue
ATYR9
AARG15
ALYS45
AGLN54
AVAL55
AGLN67
ATHR68
AASP101
AARG127
AARG131
ATYR220
ALYS221
AHOH459
AHOH518
AHOH687
AHOH742

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GTS C 240
ChainResidue
CTYR9
CPHE10
CARG15
CLYS45
CASP53
CGLN54
CVAL55
CGLN67
CTHR68
DASP101
DARG131
DHOH604

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GTS D 250
ChainResidue
CASP101
CARG131
DTYR9
DARG15
DLYS45
DGLN54
DVAL55
DPRO56
DGLN67
DTHR68
DHOH503
DHOH617
DHOH792

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues240
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues369
DetailsDomain: {"description":"GST C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11119643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
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
CTYR9

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
DTYR9

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PDB entries from 2025-10-08

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