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6CSX

Single particles Cryo-EM structure of AcrB D407A associated with lipid bilayer at 3.0 Angstrom

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 PTY B 1101
ChainResidue
APTY1101
APTY1102
BGLN439
BPTY1102
BPTY1105

site_idAC2
Number of Residues4
Detailsbinding site for residue PTY B 1102
ChainResidue
BMET1
BPHE4
BPTY1101
BPTY1105

site_idAC3
Number of Residues6
Detailsbinding site for residue PTY B 1103
ChainResidue
BARG8
BPTY1104
CGLY436
CGLN439
CALA890
CLYS955

site_idAC4
Number of Residues2
Detailsbinding site for residue PTY B 1104
ChainResidue
BPTY1103
CPTY1102

site_idAC5
Number of Residues4
Detailsbinding site for residue PTY B 1105
ChainResidue
APTY1102
APTY1103
BPTY1101
BPTY1102

site_idAC6
Number of Residues7
Detailsbinding site for residue PTY B 1106
ChainResidue
AALA22
ALEU25
ALYS29
AALA381
BSER450
BPRO455
BPHE458

site_idAC7
Number of Residues3
Detailsbinding site for residue PTY B 1107
ChainResidue
BALA22
BALA26
BALA381

site_idAC8
Number of Residues1
Detailsbinding site for residue D12 B 1108
ChainResidue
BPHE386

site_idAC9
Number of Residues4
Detailsbinding site for residue PTY C 1101
ChainResidue
APTY1103
APTY1104
CMET1
CPTY1102

site_idAD1
Number of Residues6
Detailsbinding site for residue PTY C 1102
ChainResidue
BPTY1104
CMET1
CPRO2
CLEU483
CLEU486
CPTY1101

site_idAD2
Number of Residues4
Detailsbinding site for residue PTY C 1103
ChainResidue
APHE458
CLEU25
CALA381
CALA384

site_idAD3
Number of Residues3
Detailsbinding site for residue PTY C 1104
ChainResidue
CPHE458
CPHE459
CGLY460

site_idAD4
Number of Residues7
Detailsbinding site for residue PTY A 1101
ChainResidue
APHE4
AARG8
APTY1102
BVAL443
BMET447
BCYS887
BPTY1101

site_idAD5
Number of Residues5
Detailsbinding site for residue PTY A 1102
ChainResidue
APHE4
APHE5
APTY1101
BPTY1101
BPTY1105

site_idAD6
Number of Residues3
Detailsbinding site for residue PTY A 1103
ChainResidue
AMET1
BPTY1105
CPTY1101

site_idAD7
Number of Residues5
Detailsbinding site for residue PTY A 1104
ChainResidue
AGLY440
ACYS887
ALEU891
APTY1105
CPTY1101

site_idAD8
Number of Residues3
Detailsbinding site for residue PTY A 1105
ChainResidue
AGLN439
AGLY440
APTY1104

site_idAD9
Number of Residues4
Detailsbinding site for residue PTY A 1106
ChainResidue
APHE458
AILE472
ASER476
CALA385

site_idAE1
Number of Residues2
Detailsbinding site for residue PTY A 1107
ChainResidue
AALA385
AGLY387

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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PDB entries from 2024-10-09

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