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6ZOH

3-Formylrifamycin SV binding to the access pocket of AcrB-G619P_G621P L and T protomers

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 Residues6
Detailsbinding site for residue LMT A 1201
ChainResidue
ASER530
AARG536
ASER537
AARG540
ATYR541
APHE1020

site_idAC2
Number of Residues3
Detailsbinding site for residue LMT A 1202
ChainResidue
ALEU28
ALYS29
AILE348

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 1203
ChainResidue
AGLU130
ALYS163
ASER167
AASP174
AVAL175

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 1204
ChainResidue
APRO50
AARG185
AGLU273
AGLY755
AMET774

site_idAC5
Number of Residues1
Detailsbinding site for residue D12 A 1205
ChainResidue
AALA457

site_idAC6
Number of Residues1
Detailsbinding site for residue DDQ A 1206
ChainResidue
AGLY511

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO A 1207
ChainResidue
AASP745
AARG792
AALA793

site_idAC8
Number of Residues1
Detailsbinding site for residue D12 A 1208
ChainResidue
BTRP895

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 1209
ChainResidue
ALYS55
AGLY691
AHIS692
CGLY766

site_idAD1
Number of Residues9
Detailsbinding site for residue 3YI A 1210
ChainResidue
AGLN577
APHE617
AARG620
APHE664
APHE666
AARG717
AASN719
AARG815
ALEU828

site_idAD2
Number of Residues7
Detailsbinding site for residue LMT A 1211
ChainResidue
AGLY440
AGLY444
ACYS887
AALA890
ALEU891
CARG8
CD121104

site_idAD3
Number of Residues6
Detailsbinding site for residue EDO A 1212
ChainResidue
ALEU782
CGLN229
CLEU230
CHIS596
CLYS601
EHOH204

site_idAD4
Number of Residues7
Detailsbinding site for residue LMT B 1101
ChainResidue
BSER530
BARG536
BSER537
BARG540
BTYR541
BVAL1016
DASP72

site_idAD5
Number of Residues3
Detailsbinding site for residue EDO B 1102
ChainResidue
BGLU192
BARG263
BASP264

site_idAD6
Number of Residues6
Detailsbinding site for residue GOL B 1103
ChainResidue
AARG168
AGLU309
BLEU75
BMET76
BASN820
BHOH1210

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO B 1104
ChainResidue
BPHE727
BPRO783
BSER805
BSER807

site_idAD8
Number of Residues9
Detailsbinding site for residue DDR B 1105
ChainResidue
BVAL452
BMET456
BTYR467
BTYR877
BSER880
BVAL884
BVAL905
BGLN928
BLEU932

site_idAD9
Number of Residues2
Detailsbinding site for residue DDQ B 1106
ChainResidue
APHE11
BGLY440

site_idAE1
Number of Residues7
Detailsbinding site for residue 3YI B 1107
ChainResidue
BMET575
BPHE617
BARG620
BARG717
BASN719
BARG815
BLEU828

site_idAE2
Number of Residues8
Detailsbinding site for residue PTY C 1101
ChainResidue
BTRP13
CILE882
CPHE885
CSER894
CTRP895
CSER896
CLYS950
CARG1030

site_idAE3
Number of Residues8
Detailsbinding site for residue LMT C 1102
ChainResidue
CARG536
CSER537
CARG540
CTYR541
CLEU544
CILE548
CSER530
CGLY533

site_idAE4
Number of Residues1
Detailsbinding site for residue D12 C 1103
ChainResidue
CPHE458

site_idAE5
Number of Residues2
Detailsbinding site for residue D12 C 1104
ChainResidue
ALMT1211
CMET1

site_idAE6
Number of Residues2
Detailsbinding site for residue D10 C 1105
ChainResidue
CPHE556
CILE935

site_idAE7
Number of Residues3
Detailsbinding site for residue LPX C 1106
ChainResidue
CGLY387
CPHE388
CARG468

site_idAE8
Number of Residues5
Detailsbinding site for residue EDO C 1107
ChainResidue
CGLY675
CTHR676
CALA677
CASN719
CGLU826

site_idAE9
Number of Residues1
Detailsbinding site for residue EDO C 1108
ChainResidue
CGLN89

site_idAF1
Number of Residues2
Detailsbinding site for residue EDO C 1109
ChainResidue
AGLN67
CLYS770

site_idAF2
Number of Residues2
Detailsbinding site for residue EDO C 1110
ChainResidue
CGLU339
CLYS342

site_idAF3
Number of Residues5
Detailsbinding site for residue GOL C 1112
ChainResidue
CARG185
CGLU273
CGLY755
CGLY756
CMET774

site_idAF4
Number of Residues3
Detailsbinding site for residue LMT C 1113
ChainResidue
CLYS29
CALA384
CALA385

site_idAF5
Number of Residues2
Detailsbinding site for residue LMT C 1114
ChainResidue
CGLY511
CPHE512

site_idAF6
Number of Residues1
Detailsbinding site for residue HEX C 1115
ChainResidue
CSER530

site_idAF7
Number of Residues4
Detailsbinding site for residue GOL C 1116
ChainResidue
CGLU593
CHIS596
CTYR597
CLYS601

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 Residues1932
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 Residues57
DetailsTransmembrane: {"description":"Helical; Name=11"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues57
DetailsTransmembrane: {"description":"Helical; Name=12"}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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