Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5NC5

Crystal structure of AcrBZ in complex with antibiotic puromycin

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
F0005886cellular_componentplasma membrane
F0042910molecular_functionxenobiotic transmembrane transporter activity
F0046677biological_processresponse to antibiotic
F1990961biological_processxenobiotic detoxification by transmembrane export across the plasma membrane
G0005886cellular_componentplasma membrane
G0042910molecular_functionxenobiotic transmembrane transporter activity
G0046677biological_processresponse to antibiotic
G1990961biological_processxenobiotic detoxification by transmembrane export across the plasma membrane
H0005886cellular_componentplasma membrane
H0042910molecular_functionxenobiotic transmembrane transporter activity
H0046677biological_processresponse to antibiotic
H1990961biological_processxenobiotic detoxification by transmembrane export across the plasma membrane
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue LMT A 1101
ChainResidue
AILE27
ALEU28
ALEU30
AVAL32
AHIS338
APHE380
AD101106

site_idAC2
Number of Residues1
Detailsbinding site for residue LMT A 1102
ChainResidue
CILE18

site_idAC3
Number of Residues2
Detailsbinding site for residue D12 A 1103
ChainResidue
AMET20
ATRP13

site_idAC4
Number of Residues2
Detailsbinding site for residue D10 A 1104
ChainResidue
ATRP895
AD101105

site_idAC5
Number of Residues3
Detailsbinding site for residue D10 A 1105
ChainResidue
APHE885
ATRP895
AD101104

site_idAC6
Number of Residues2
Detailsbinding site for residue D10 A 1106
ChainResidue
AILE370
ALMT1101

site_idAC7
Number of Residues3
Detailsbinding site for residue D10 A 1108
ChainResidue
AALA457
APHE458
ADD91110

site_idAC8
Number of Residues2
Detailsbinding site for residue D10 A 1109
ChainResidue
AALA385
ADD91114

site_idAC9
Number of Residues2
Detailsbinding site for residue DD9 A 1110
ChainResidue
APHE386
AD101108

site_idAD1
Number of Residues4
Detailsbinding site for residue LMT A 1111
ChainResidue
ALYS29
ADD91113
BSER450
BVAL454

site_idAD2
Number of Residues1
Detailsbinding site for residue D12 A 1112
ChainResidue
AARG8

site_idAD3
Number of Residues1
Detailsbinding site for residue DD9 A 1113
ChainResidue
ALMT1111

site_idAD4
Number of Residues2
Detailsbinding site for residue DD9 A 1114
ChainResidue
AD101109
BDD91112

site_idAD5
Number of Residues1
Detailsbinding site for residue D10 B 1101
ChainResidue
BTRP895

site_idAD6
Number of Residues3
Detailsbinding site for residue D10 B 1103
ChainResidue
BTRP13
BD101110
CTRP895

site_idAD7
Number of Residues1
Detailsbinding site for residue D10 B 1105
ChainResidue
BPHE885

site_idAD8
Number of Residues1
Detailsbinding site for residue DD9 B 1106
ChainResidue
CD101104

site_idAD9
Number of Residues2
Detailsbinding site for residue DD9 B 1107
ChainResidue
BLEU25
CILE879

site_idAE1
Number of Residues1
Detailsbinding site for residue D10 B 1110
ChainResidue
BD101103

site_idAE2
Number of Residues3
Detailsbinding site for residue D10 B 1111
ChainResidue
BTYR467
BTYR877
BGLN928

site_idAE3
Number of Residues2
Detailsbinding site for residue DD9 B 1112
ChainResidue
ADD91114
BDD91119

site_idAE4
Number of Residues2
Detailsbinding site for residue D10 B 1113
ChainResidue
BPHE386
BSER476

site_idAE5
Number of Residues2
Detailsbinding site for residue D10 B 1114
ChainResidue
BPHE4
BD101122

site_idAE6
Number of Residues2
Detailsbinding site for residue DD9 B 1115
ChainResidue
BSER875
BILE882

site_idAE7
Number of Residues2
Detailsbinding site for residue D10 B 1116
ChainResidue
BSER880
BLEU881

site_idAE8
Number of Residues3
Detailsbinding site for residue D10 B 1117
ChainResidue
BILE27
BPHE380
BILE390

site_idAE9
Number of Residues2
Detailsbinding site for residue DD9 B 1119
ChainResidue
BALA385
BDD91112

site_idAF1
Number of Residues9
Detailsbinding site for residue PUY B 1120
ChainResidue
BSER134
BPHE136
BVAL139
BPHE178
BMET573
BPHE617
BPHE666
BLEU668
BVAL672

site_idAF2
Number of Residues4
Detailsbinding site for residue D12 B 1121
ChainResidue
BARG8
CMET447
CALA890
CLEU891

site_idAF3
Number of Residues1
Detailsbinding site for residue D10 B 1122
ChainResidue
BD101114

site_idAF4
Number of Residues2
Detailsbinding site for residue DD9 C 1101
ChainResidue
CPHE458
CD121108

site_idAF5
Number of Residues1
Detailsbinding site for residue D12 C 1103
ChainResidue
CTRP895

site_idAF6
Number of Residues2
Detailsbinding site for residue D10 C 1104
ChainResidue
BDD91106
CPHE458

site_idAF7
Number of Residues2
Detailsbinding site for residue D12 C 1106
ChainResidue
ATRP895
CTRP13

site_idAF8
Number of Residues1
Detailsbinding site for residue D12 C 1107
ChainResidue
CPHE458

site_idAF9
Number of Residues1
Detailsbinding site for residue D12 C 1108
ChainResidue
CDD91101

site_idAG1
Number of Residues1
Detailsbinding site for residue DD9 C 1109
ChainResidue
CDD91110

site_idAG2
Number of Residues1
Detailsbinding site for residue DD9 C 1110
ChainResidue
CDD91109

site_idAG3
Number of Residues1
Detailsbinding site for residue D10 C 1112
ChainResidue
CGLN439

site_idAG4
Number of Residues2
Detailsbinding site for residue D10 C 1115
ChainResidue
CPHE885
CD101116

site_idAG5
Number of Residues2
Detailsbinding site for residue D10 C 1116
ChainResidue
CMET902
CD101115

site_idAG6
Number of Residues1
Detailsbinding site for residue D10 C 1117
ChainResidue
CLEU881

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

site_idSWS_FT_FI15
Number of Residues18
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues60
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01484","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon