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6ZO9

Binding of two rifabutins to the access pocket of AcrB-G621P T protomer

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0015562molecular_functionefflux transmembrane transporter activity
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0042802molecular_functionidentical protein binding
A0042908biological_processxenobiotic transport
A0042910molecular_functionxenobiotic transmembrane transporter activity
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
B0015562molecular_functionefflux transmembrane transporter activity
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0042802molecular_functionidentical protein binding
B0042908biological_processxenobiotic transport
B0042910molecular_functionxenobiotic transmembrane transporter activity
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
C0015562molecular_functionefflux transmembrane transporter activity
C0016020cellular_componentmembrane
C0022857molecular_functiontransmembrane transporter activity
C0042802molecular_functionidentical protein binding
C0042908biological_processxenobiotic transport
C0042910molecular_functionxenobiotic transmembrane transporter activity
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 Residues1
Detailsbinding site for residue D12 A 1101
ChainResidue
AALA457

site_idAC2
Number of Residues3
Detailsbinding site for residue LMT A 1102
ChainResidue
ALEU28
ALYS29
AVAL32

site_idAC3
Number of Residues5
Detailsbinding site for residue LMT A 1103
ChainResidue
AGLY440
ACYS887
AALA890
ALEU891
CARG8

site_idAC4
Number of Residues5
Detailsbinding site for residue LMT A 1104
ChainResidue
ASER530
AGLY533
AARG536
AARG540
ATYR541

site_idAC5
Number of Residues3
Detailsbinding site for residue PTY A 1105
ChainResidue
APHE4
AILE18
BGLY440

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL A 1106
ChainResidue
ATYR811
EGLU20
EASP44
EHOH203

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO A 1107
ChainResidue
APRO36
ATHR37
ASER389

site_idAC8
Number of Residues7
Detailsbinding site for residue LMT B 1101
ChainResidue
BSER530
BILE534
BARG536
BSER537
BTYR541
BPHE1020
DASP72

site_idAC9
Number of Residues6
Detailsbinding site for residue DDR B 1102
ChainResidue
BVAL452
BTYR467
BTYR877
BSER880
BGLN928
BLEU932

site_idAD1
Number of Residues1
Detailsbinding site for residue HEX B 1103
ChainResidue
BTRP895

site_idAD2
Number of Residues1
Detailsbinding site for residue OCT B 1105
ChainResidue
BPHE885

site_idAD3
Number of Residues3
Detailsbinding site for residue GOL B 1106
ChainResidue
AALA165
AARG168
BASN820

site_idAD4
Number of Residues4
Detailsbinding site for residue SO4 B 1107
ChainResidue
BLYS55
BGLY691
BHIS692
BHOH1203

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO B 1108
ChainResidue
BSER233
BHOH1223
CSER84
CPRO621
CPRO814

site_idAD6
Number of Residues2
Detailsbinding site for residue EDO B 1109
ChainResidue
BTHR463
BGLU866

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO B 1110
ChainResidue
APHE316
BALA688
BTHR853
BGLY854

site_idAD8
Number of Residues16
Detailsbinding site for residue RBT B 1111
ChainResidue
BMET575
BPHE664
BPHE666
BTHR676
BTHR678
BPHE680
BASP681
BSER715
BPRO718
BASN719
BGLY720
BGLU826
BLEU828
BGLY829
BGLN830
BRBT1112

site_idAD9
Number of Residues9
Detailsbinding site for residue RBT B 1112
ChainResidue
BMET575
BPHE617
BALA618
BPHE666
BPRO669
BLEU674
BGLY675
BASN719
BRBT1111

site_idAE1
Number of Residues1
Detailsbinding site for residue D10 C 1102
ChainResidue
CILE935

site_idAE2
Number of Residues5
Detailsbinding site for residue LMT C 1106
ChainResidue
CSER530
CARG536
CSER537
CARG540
CTYR541

site_idAE3
Number of Residues3
Detailsbinding site for residue LMT C 1107
ChainResidue
CGLY511
CPHE512
CARG518

site_idAE4
Number of Residues9
Detailsbinding site for residue PTY C 1108
ChainResidue
CHOH1215
BTRP13
CILE882
CSER894
CTRP895
CSER896
CLYS950
CARG1030
CSER1034

site_idAE5
Number of Residues8
Detailsbinding site for residue PTY C 1109
ChainResidue
BARG8
BPHE11
BILE18
CGLY440
CMET447
CLEU891
CTYR892
CLYS950

site_idAE6
Number of Residues1
Detailsbinding site for residue OCT C 1111
ChainResidue
CSER530

site_idAE7
Number of Residues4
Detailsbinding site for residue GOL C 1112
ChainResidue
CLEU564
CPRO565
CASP566
CSER836

site_idAE8
Number of Residues3
Detailsbinding site for residue SO4 C 1113
ChainResidue
CLYS55
CGLY691
CHIS692

site_idAE9
Number of Residues1
Detailsbinding site for residue CL C 1114
ChainResidue
CARG468

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues462
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15919996
ChainResidueDetails
AMET1-PRO9
ALEU357-THR365
AGLU414-ILE438
AALA491-THR538
AALA889-PRO898
ALEU944-LEU972
AILE1019-HIS1049
BMET1-PRO9
BLEU357-THR365
BGLU414-ILE438
BALA491-THR538
BALA889-PRO898
BLEU944-LEU972
BILE1019-HIS1049
CMET1-PRO9
CLEU357-THR365
CGLU414-ILE438
CALA491-THR538
CALA889-PRO898
CLEU944-LEU972
CILE1019-HIS1049

site_idSWS_FT_FI2
Number of Residues54
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AILE10-LEU28
BILE10-LEU28
CILE10-LEU28

site_idSWS_FT_FI3
Number of Residues1932
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:15919996
ChainResidueDetails
ALYS29-SER336
APHE386-ASN391
APHE458-ALA465
APHE556-ASN871
AARG919-ASP924
ATHR993-GLY998
BLYS29-SER336
BPHE386-ASN391
BPHE458-ALA465
BPHE556-ASN871
BARG919-ASP924
BTHR993-GLY998
CLYS29-SER336
CPHE386-ASN391
CPHE458-ALA465
CPHE556-ASN871
CARG919-ASP924
CTHR993-GLY998

site_idSWS_FT_FI4
Number of Residues57
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
AILE337-TYR356
BILE337-TYR356
CILE337-TYR356

site_idSWS_FT_FI5
Number of Residues57
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
ALEU366-ALA385
BLEU366-ALA385
CLEU366-ALA385

site_idSWS_FT_FI6
Number of Residues63
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
ATHR392-VAL413
BTHR392-VAL413
CTHR392-VAL413

site_idSWS_FT_FI7
Number of Residues54
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AGLN439-ALA457
BGLN439-ALA457
CGLN439-ALA457

site_idSWS_FT_FI8
Number of Residues72
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
AILE466-PRO490
BILE466-PRO490
CILE466-PRO490

site_idSWS_FT_FI9
Number of Residues48
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
AGLY539-LEU555
BGLY539-LEU555
CGLY539-LEU555

site_idSWS_FT_FI10
Number of Residues48
DetailsTRANSMEM: Helical; Name=8
ChainResidueDetails
AGLN872-LEU888
BGLN872-LEU888
CGLN872-LEU888

site_idSWS_FT_FI11
Number of Residues57
DetailsTRANSMEM: Helical; Name=9
ChainResidueDetails
APHE899-PHE918
BPHE899-PHE918
CPHE899-PHE918

site_idSWS_FT_FI12
Number of Residues54
DetailsTRANSMEM: Helical; Name=10
ChainResidueDetails
AVAL925-ILE943
BVAL925-ILE943
CVAL925-ILE943

site_idSWS_FT_FI13
Number of Residues57
DetailsTRANSMEM: Helical; Name=11
ChainResidueDetails
AARG973-SER992
BARG973-SER992
CARG973-SER992

site_idSWS_FT_FI14
Number of Residues57
DetailsTRANSMEM: Helical; Name=12
ChainResidueDetails
AALA999-ALA1018
BALA999-ALA1018
CALA999-ALA1018

221051

PDB entries from 2024-06-12

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