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6GSU

FIRST-SPHERE AND SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE ACTIVE SITE OF A CLASS MU GLUTATHIONE TRANSFERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005496molecular_functionsteroid binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0006749biological_processglutathione metabolic process
A0007608biological_processsensory perception of smell
A0010038biological_processresponse to metal ion
A0010288biological_processresponse to lead ion
A0016151molecular_functionnickel cation binding
A0016740molecular_functiontransferase activity
A0018916biological_processnitrobenzene metabolic process
A0019899molecular_functionenzyme binding
A0019901molecular_functionprotein kinase binding
A0032991cellular_componentprotein-containing complex
A0042178biological_processxenobiotic catabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043200biological_processresponse to amino acid
A0043295molecular_functionglutathione binding
A0045471biological_processresponse to ethanol
A0048678biological_processresponse to axon injury
A0051122biological_processhepoxilin biosynthetic process
A0070458biological_processcellular detoxification of nitrogen compound
A0071466biological_processcellular response to xenobiotic stimulus
A1901687biological_processglutathione derivative biosynthetic process
B0004364molecular_functionglutathione transferase activity
B0005496molecular_functionsteroid binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006693biological_processprostaglandin metabolic process
B0006749biological_processglutathione metabolic process
B0007608biological_processsensory perception of smell
B0010038biological_processresponse to metal ion
B0010288biological_processresponse to lead ion
B0016151molecular_functionnickel cation binding
B0016740molecular_functiontransferase activity
B0018916biological_processnitrobenzene metabolic process
B0019899molecular_functionenzyme binding
B0019901molecular_functionprotein kinase binding
B0032991cellular_componentprotein-containing complex
B0042178biological_processxenobiotic catabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043200biological_processresponse to amino acid
B0043295molecular_functionglutathione binding
B0045471biological_processresponse to ethanol
B0048678biological_processresponse to axon injury
B0051122biological_processhepoxilin biosynthetic process
B0070458biological_processcellular detoxification of nitrogen compound
B0071466biological_processcellular response to xenobiotic stimulus
B1901687biological_processglutathione derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GPS A 221
ChainResidue
ATYR6
ASER72
AMET108
AILE111
APHE208
BASP105
AHOH223
AHOH236
AHOH270
AHOH307
AHOH311
ATRP7
AHOH326
AHOH345
AHOH388
AGLY11
ALEU12
ATRP45
ALYS49
AASN58
ALEU59
AGLN71

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GPS B 218
ChainResidue
AASP105
BTYR6
BTRP7
BGLY11
BLEU12
BTRP45
BLYS49
BASN58
BLEU59
BGLN71
BSER72
BMET108
BILE111
BPHE208
BHOH219
BHOH220
AHOH244
BHOH274
BHOH292
BHOH297
BHOH305
BHOH312
BHOH323
BHOH336

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 218
ChainResidue
AARG201
AHOH292
AHOH330
AHOH385

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 219
ChainResidue
AASP105
AGLN109

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 220
ChainResidue
AHOH310

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues172
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues236
DetailsDomain: {"description":"GST C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8664265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8110735","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
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

238895

PDB entries from 2025-07-16

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