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5G5A

Glutathione transferase U25 from Arabidopsis thaliana in complex with glutathione disulfide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006749biological_processglutathione metabolic process
A0009407biological_processtoxin catabolic process
A0009636biological_processresponse to toxic substance
A0016740molecular_functiontransferase activity
A0046256biological_process2,4,6-trinitrotoluene catabolic process
B0004364molecular_functionglutathione transferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006749biological_processglutathione metabolic process
B0009407biological_processtoxin catabolic process
B0009636biological_processresponse to toxic substance
B0016740molecular_functiontransferase activity
B0046256biological_process2,4,6-trinitrotoluene catabolic process
C0004364molecular_functionglutathione transferase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006749biological_processglutathione metabolic process
C0009407biological_processtoxin catabolic process
C0009636biological_processresponse to toxic substance
C0016740molecular_functiontransferase activity
C0046256biological_process2,4,6-trinitrotoluene catabolic process
D0004364molecular_functionglutathione transferase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006749biological_processglutathione metabolic process
D0009407biological_processtoxin catabolic process
D0009636biological_processresponse to toxic substance
D0016740molecular_functiontransferase activity
D0046256biological_process2,4,6-trinitrotoluene catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBinding site for residues GSH A1221 and GSH A1222
ChainResidue
ASER13
AARG111
AHOH2010
AHOH2064
AHOH2071
AHOH2111
AHOH2189
AHOH2190
APHE15
ALYS40
ALYS53
AILE54
APRO55
AGLU66
ASER67
ATYR107

site_idAC2
Number of Residues17
DetailsBinding site for residues GSH B1221 and GSH B1222
ChainResidue
BSER13
BPHE15
BLYS40
BLYS53
BILE54
BPRO55
BGLU66
BSER67
BTYR107
BARG111
BHOH2088
BHOH2096
BHOH2129
BHOH2204
BHOH2205
BHOH2206
BHOH2207

site_idAC3
Number of Residues17
DetailsBinding site for residues GSH C1221 and GSH C1222
ChainResidue
CSER13
CPHE15
CLYS40
CLYS53
CILE54
CPRO55
CGLU66
CSER67
CTYR107
CARG111
CHOH2012
CHOH2057
CHOH2105
CHOH2168
CHOH2169
CHOH2170
DLYS104

site_idAC4
Number of Residues19
DetailsBinding site for residues GSH D1221 and GSH D1222
ChainResidue
CLYS104
CHOH2108
DSER13
DPHE15
DLEU37
DLYS40
DLYS53
DILE54
DPRO55
DGLU66
DSER67
DTYR107
DARG111
DHOH2027
DHOH2043
DHOH2047
DHOH2149
DHOH2150
DHOH2151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER13
CASN39
CLYS53
CGLU66
DSER13
DASN39
DLYS53
DGLU66
AASN39
ALYS53
AGLU66
BSER13
BASN39
BLYS53
BGLU66
CSER13

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895
ChainResidueDetails
AALA2
BALA2
CALA2
DALA2

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9ZW27
ChainResidueDetails
ATHR149
BTHR149
CTHR149
DTHR149

226707

PDB entries from 2024-10-30

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