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6ZOD

Fusidic acid binding to the allosteric deep transmembrane domain binding pocket, TM7/TM8 groove, and TM1/TM2 groove of the fully induced AcrB T protomer

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0009410biological_processresponse to xenobiotic stimulus
A0009636biological_processresponse to toxic substance
A0015125molecular_functionbile acid transmembrane transporter activity
A0015562molecular_functionefflux transmembrane transporter activity
A0015567molecular_functionalkane transmembrane transporter activity
A0015721biological_processbile acid and bile salt transport
A0015895biological_processalkane transport
A0015908biological_processfatty acid transport
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0042802molecular_functionidentical protein binding
A0042908biological_processxenobiotic transport
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0042930biological_processenterobactin transport
A0042931molecular_functionenterobactin transmembrane transporter activity
A0046677biological_processresponse to antibiotic
A0055085biological_processtransmembrane transport
A0098567cellular_componentperiplasmic side of plasma membrane
A0140330biological_processxenobiotic detoxification by transmembrane export across the cell outer membrane
A1990281cellular_componentefflux pump complex
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0009410biological_processresponse to xenobiotic stimulus
B0009636biological_processresponse to toxic substance
B0015125molecular_functionbile acid transmembrane transporter activity
B0015562molecular_functionefflux transmembrane transporter activity
B0015567molecular_functionalkane transmembrane transporter activity
B0015721biological_processbile acid and bile salt transport
B0015895biological_processalkane transport
B0015908biological_processfatty acid transport
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0042802molecular_functionidentical protein binding
B0042908biological_processxenobiotic transport
B0042910molecular_functionxenobiotic transmembrane transporter activity
B0042930biological_processenterobactin transport
B0042931molecular_functionenterobactin transmembrane transporter activity
B0046677biological_processresponse to antibiotic
B0055085biological_processtransmembrane transport
B0098567cellular_componentperiplasmic side of plasma membrane
B0140330biological_processxenobiotic detoxification by transmembrane export across the cell outer membrane
B1990281cellular_componentefflux pump complex
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0009410biological_processresponse to xenobiotic stimulus
C0009636biological_processresponse to toxic substance
C0015125molecular_functionbile acid transmembrane transporter activity
C0015562molecular_functionefflux transmembrane transporter activity
C0015567molecular_functionalkane transmembrane transporter activity
C0015721biological_processbile acid and bile salt transport
C0015895biological_processalkane transport
C0015908biological_processfatty acid transport
C0016020cellular_componentmembrane
C0022857molecular_functiontransmembrane transporter activity
C0042802molecular_functionidentical protein binding
C0042908biological_processxenobiotic transport
C0042910molecular_functionxenobiotic transmembrane transporter activity
C0042930biological_processenterobactin transport
C0042931molecular_functionenterobactin transmembrane transporter activity
C0046677biological_processresponse to antibiotic
C0055085biological_processtransmembrane transport
C0098567cellular_componentperiplasmic side of plasma membrane
C0140330biological_processxenobiotic detoxification by transmembrane export across the cell outer membrane
C1990281cellular_componentefflux pump complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue LMT A 1101
ChainResidue
AILE27
AVAL341
ALEU377
ALMT1112
AFUA1113

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 1102
ChainResidue
ATYR758
ALYS770

site_idAC3
Number of Residues8
Detailsbinding site for residue LMT A 1103
ChainResidue
BGLN439
BGLY440
BMET447
BALA890
BLEU891
BLYS955
AARG8
AILE18

site_idAC4
Number of Residues2
Detailsbinding site for residue EDO A 1104
ChainResidue
AGLN125
AGLY126

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 1105
ChainResidue
ASER84
AALA580
AGLY581
CASN231
CALA232
CSER233

site_idAC6
Number of Residues1
Detailsbinding site for residue EDO A 1109
ChainResidue
ALYS589

site_idAC7
Number of Residues6
Detailsbinding site for residue LMT A 1111
ChainResidue
AGLY440
AGLY444
AMET447
AALA890
ALEU891
CARG8

site_idAC8
Number of Residues4
Detailsbinding site for residue LMT A 1112
ChainResidue
ALYS29
ALMT1101
BASN871
BGLN872

site_idAC9
Number of Residues4
Detailsbinding site for residue FUA A 1113
ChainResidue
ALEU28
ALYS334
AHIS338
ALMT1101

site_idAD1
Number of Residues1
Detailsbinding site for residue EDO B 1201
ChainResidue
BSER233

site_idAD2
Number of Residues2
Detailsbinding site for residue GOL B 1202
ChainResidue
BGLN176
BLYS292

site_idAD3
Number of Residues3
Detailsbinding site for residue PGE B 1204
ChainResidue
BPHE617
BTHR678
BARG717

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO B 1205
ChainResidue
BLYS248
BARG259
BARG263

site_idAD5
Number of Residues4
Detailsbinding site for residue EDO B 1206
ChainResidue
ALYS312
BGLN687
BASN820
BASP858

site_idAD6
Number of Residues5
Detailsbinding site for residue 8K6 B 1208
ChainResidue
BILE27
BASN298
BASP301
BPHE380
BFUA1214

site_idAD7
Number of Residues2
Detailsbinding site for residue SO4 B 1209
ChainResidue
AARG168
BASN820

site_idAD8
Number of Residues2
Detailsbinding site for residue SO4 B 1210
ChainResidue
BPRO36
BTHR37

site_idAD9
Number of Residues4
Detailsbinding site for residue SO4 B 1211
ChainResidue
BASN361
BPHE362
BARG363
BLYS498

site_idAE1
Number of Residues3
Detailsbinding site for residue SO4 B 1212
ChainResidue
BLYS55
BGLY691
BHIS692

site_idAE2
Number of Residues11
Detailsbinding site for residue FUA B 1213
ChainResidue
BVAL452
BTYR545
BMET552
BTYR877
BSER880
BLEU881
BVAL884
BMET902
BLEU903
BPRO906
BLEU932

site_idAE3
Number of Residues4
Detailsbinding site for residue FUA B 1214
ChainResidue
BLEU300
BLYS334
BHIS338
B8K61208

site_idAE4
Number of Residues7
Detailsbinding site for residue FUA B 1215
ChainResidue
BGLU346
BALA347
BVAL399
BGLY930
BTHR934
BPHE982
BGLY985

site_idAE5
Number of Residues3
Detailsbinding site for residue EDO C 1301
ChainResidue
BASP761
CGLN120
CGLU121

site_idAE6
Number of Residues3
Detailsbinding site for residue LMT C 1302
ChainResidue
CLEU28
CLEU30
CVAL32

site_idAE7
Number of Residues6
Detailsbinding site for residue PTY C 1303
ChainResidue
CLYS950
CARG1030
BTHR495
CSER894
CTRP895
CSER896

site_idAE8
Number of Residues1
Detailsbinding site for residue EDO C 1304
ChainResidue
CASN820

site_idAE9
Number of Residues2
Detailsbinding site for residue LMT C 1305
ChainResidue
CALA385
CD121308

site_idAF1
Number of Residues8
Detailsbinding site for residue LMT C 1306
ChainResidue
CSER530
CGLY533
CILE534
CARG536
CSER537
CTYR541
CLEU544
CILE548

site_idAF2
Number of Residues2
Detailsbinding site for residue PTY C 1307
ChainResidue
CPRO455
CPHE458

site_idAF3
Number of Residues1
Detailsbinding site for residue D12 C 1308
ChainResidue
CLMT1305

site_idAF4
Number of Residues1
Detailsbinding site for residue HEX C 1309
ChainResidue
CPHE386

site_idAF5
Number of Residues3
Detailsbinding site for residue SO4 C 1310
ChainResidue
CLYS55
CGLY691
CHIS692

site_idAF6
Number of Residues3
Detailsbinding site for residue EDO D 201
ChainResidue
BTYR811
DARG23
DASP44

site_idAF7
Number of Residues1
Detailsbinding site for residue EDO D 202
ChainResidue
DARG23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues372
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1927
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues57
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues57
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues63
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues72
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=8"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues57
DetailsTransmembrane: {"description":"Helical; Name=9"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=10"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=11"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=12"}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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