Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6GSW

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
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
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
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 Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 218
ChainResidue
ALYS49
AGPS221

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 219
ChainResidue
AASP105
AGLN109
AHOH360
AHOH416

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 220
ChainResidue
ALYS51
ATYR202
ASER204

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GPS A 221
ChainResidue
ATYR6
ATRP7
AGLY11
AARG42
ATRP45
ALYS49
AASN58
ALEU59
APRO60
AGLN71
ASER72
AARG107
AILE111
ASER209
ASO4218
AHOH224
AHOH232
AHOH302
AHOH331
BASP105

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GPS B 218
ChainResidue
AASP105
AHOH250
AHOH416
BTYR6
BTRP7
BLEU12
BTRP45
BLYS49
BASN58
BLEU59
BPRO60
BGLN71
BSER72
BHOH219
BHOH221
BHOH311
BHOH316

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

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

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon