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6GST

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

Replaces:  1GST
Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005496molecular_functionsteroid binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0006749biological_processglutathione metabolic process
A0007608biological_processsensory perception of smell
A0009410biological_processresponse to xenobiotic stimulus
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
A0050896biological_processresponse to stimulus
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
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006693biological_processprostaglandin metabolic process
B0006749biological_processglutathione metabolic process
B0007608biological_processsensory perception of smell
B0009410biological_processresponse to xenobiotic stimulus
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
B0050896biological_processresponse to stimulus
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 Residues16
DetailsBINDING SITE FOR RESIDUE GSH A 218
ChainResidue
ATYR6
AHOH221
AHOH223
AHOH239
AHOH277
AHOH351
AHOH413
AHOH414
ATRP7
ATRP45
ALYS49
AASN58
ALEU59
AGLN71
ASER72
BASP105

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GSH B 218
ChainResidue
AASP105
BTYR6
BTRP7
BTRP45
BLYS49
BASN58
BLEU59
BGLN71
BSER72
BHOH221
BHOH222
BHOH261
BHOH266
BHOH278
BHOH307
BHOH321
BHOH353
BHOH386

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:8664265, ECO:0000305|PubMed:8110735
ChainResidueDetails
APHE50
ALEU59
ASER72
BTRP7
BSER43
BPHE50
BLEU59
BSER72
ATRP7
ASER43

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN116
BASN116

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
AARG67
ATHR205
ALYS210
BARG67
BTHR205
BLYS210

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PDB entries from 2024-04-17

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