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6ZO7

3-Formylrifamycin SV binding to the access pocket of AcrB-G619P L and 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 Residues7
Detailsbinding site for residue LMT A 1201
ChainResidue
AGLY440
AMET447
AALA890
ALEU891
CARG8
CPHE11
CILE18

site_idAC2
Number of Residues3
Detailsbinding site for residue LMT A 1202
ChainResidue
AHOH1334
ALEU28
AHIS338

site_idAC3
Number of Residues6
Detailsbinding site for residue LMT A 1203
ChainResidue
ASER530
AARG536
ASER537
AARG540
ATYR541
APHE1020

site_idAC4
Number of Residues1
Detailsbinding site for residue D10 A 1204
ChainResidue
ATRP895

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 1205
ChainResidue
AASP761
AVAL768
ALYS770
BGLN67

site_idAC6
Number of Residues7
Detailsbinding site for residue LMT A 1206
ChainResidue
ATYR467
APHE556
APHE563
AASN871
ATYR877
AASN923
AGLN928

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 1207
ChainResidue
AASN231
ASER233
BSER84
BTHR724

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO A 1208
ChainResidue
AGLN124
ATYR758
AVAL759
AASN760
AASP761

site_idAC9
Number of Residues9
Detailsbinding site for residue 3YI A 1209
ChainResidue
AMET575
APHE617
AARG620
APHE664
APHE666
AARG717
AASN719
AARG815
ALEU828

site_idAD1
Number of Residues4
Detailsbinding site for residue LMT A 1210
ChainResidue
AARG8
BGLY440
BMET447
BCYS887

site_idAD2
Number of Residues2
Detailsbinding site for residue EDO A 1211
ChainResidue
AASN74
CTHR295

site_idAD3
Number of Residues5
Detailsbinding site for residue LMT B 1201
ChainResidue
BSER530
BARG536
BARG540
BTYR541
DASP72

site_idAD4
Number of Residues5
Detailsbinding site for residue GOL B 1202
ChainResidue
BGLN124
BARG239
BASP761
CGLN120
CGLU121

site_idAD5
Number of Residues4
Detailsbinding site for residue LMT B 1204
ChainResidue
BLYS510
BGLY511
BPHE512
BTRP515

site_idAD6
Number of Residues2
Detailsbinding site for residue EDO B 1205
ChainResidue
BTHR528
BARG969

site_idAD7
Number of Residues13
Detailsbinding site for residue 3YI B 1206
ChainResidue
BMET573
BMET575
BPHE617
BARG620
BLEU668
BPRO669
BVAL672
BARG717
BPRO718
BASN719
BGLY720
BARG815
BLEU828

site_idAD8
Number of Residues4
Detailsbinding site for residue SO4 B 1207
ChainResidue
BASN361
BPHE362
BARG363
BLYS498

site_idAD9
Number of Residues7
Detailsbinding site for residue PTY C 1101
ChainResidue
BMET20
CSER894
CTRP895
CSER896
CLYS950
CSER1034
CHOH1212

site_idAE1
Number of Residues6
Detailsbinding site for residue LMT C 1102
ChainResidue
CSER530
CGLY533
CARG536
CSER537
CARG540
CTYR541

site_idAE2
Number of Residues6
Detailsbinding site for residue LMT C 1105
ChainResidue
CLYS342
CILE991
CSER992
CTHR993
CGLY994
CGLU339

site_idAE3
Number of Residues8
Detailsbinding site for residue PTY C 1106
ChainResidue
BARG8
BPHE11
CGLN439
CALA890
CLEU891
CTYR892
CLYS950
CASP954

site_idAE4
Number of Residues1
Detailsbinding site for residue R16 C 1107
ChainResidue
CPHE458

site_idAE5
Number of Residues3
Detailsbinding site for residue EDO C 1109
ChainResidue
CASP153
CASP156
CARG765

site_idAE6
Number of Residues5
Detailsbinding site for residue GOL C 1110
ChainResidue
AGLY51
AGLY755
AMET774
CGLY221
CTHR222

site_idAE7
Number of Residues2
Detailsbinding site for residue DDQ C 1111
ChainResidue
CARG468
CSER471

site_idAE8
Number of Residues3
Detailsbinding site for residue LMT C 1112
ChainResidue
CGLY511
CTRP515
CARG518

site_idAE9
Number of Residues4
Detailsbinding site for residue EDO C 1113
ChainResidue
CTRP187
CGLU776
CALA777
CHOH1247

site_idAF1
Number of Residues2
Detailsbinding site for residue NA C 1114
ChainResidue
CPHE358
CGLN360

site_idAF2
Number of Residues4
Detailsbinding site for residue GOL E 201
ChainResidue
ATYR811
EGLU20
EARG23
EASP44

site_idAF3
Number of Residues2
Detailsbinding site for residue EDO E 202
ChainResidue
EASP143
ELYS147

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 Residues57
DetailsTransmembrane: {"description":"Helical; Name=12"}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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