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• 1IWG: crystal structure of bacterial multidrug efflux transporter acrb (10.1038/NATURE01050 )
• 1OY6: structural basis of the multiple binding capacity of the acrb multidrug efflux pump (10.1126/SCIENCE.1083137 )
• 1OY8: structural basis of multiple drug binding capacity of the acrb multidrug efflux pump (10.1126/SCIENCE.1083137 )
• 1OY9: structural basis of multiple drug binding capacity of the acrb multidrug efflux pump (10.1126/SCIENCE.1083137 )
• 1OYD: structural basis of multiple binding capacity of the acrb multidrug efflux pump (10.1126/SCIENCE.1083137 )
• 1OYE: structural basis of multiple binding capacity of the acrb multidrug efflux pump (10.1126/SCIENCE.1083137 )
• 1T9T: structural basis of multidrug transport by the acrb multidrug efflux pump (10.1128/JB.187.19.6804-6815.2005 )
• 1T9U: structural basis of multidrug transport by the acrb multidrug efflux pump (10.1128/JB.187.19.6804-6815.2005 )
• 1T9V: structural basis of multidrug transport by the acrb multidrug efflux pump (10.1128/JB.187.19.6804-6815.2005 )
• 1T9W: structural basis of multidrug transport by the acrb multidrug efflux pump (10.1128/JB.187.19.6804-6815.2005 )
• 1T9X: structural basis of multidrug transport by the acrb multidrug efflux pump (10.1128/JB.187.19.6804-6815.2005 )
• 1T9Y: structural basis of multidrug transport by the acrb multidrug efflux pump (10.1128/JB.187.19.6804-6815.2005 )
• 2DHH: crystal structure of a multidrug transporter reveal a functionally rotating mechanism (10.1038/NATURE05076 )
• 2DR6: crystal structure of a multidrug transporter reveal a functionally rotating mechanism (10.1038/NATURE05076 )
• 2DRD: crystal structure of a multidrug transporter reveal a functionally rotating mechanism (10.1038/NATURE05076 )
• 2GIF: asymmetric structure of trimeric acrb from escherichia coli (10.1126/SCIENCE.1131542 )
• 2HQC: conformation of the acrb multidrug efflux pump in mutants of the putative proton relay pathway (10.1128/JB.00684-06 )
• 2HQD: conformation of the acrb multidrug efflux pump in mutants of the putative proton relay pathway (10.1128/JB.00684-06 )
• 2HQF: conformation of the acrb multidrug efflux pump in mutants of the putative proton relay pathway (10.1128/JB.00684-06 )
• 2HQG: conformation of the acrb multidrug efflux pump in mutants of the putative proton relay pathway (10.1128/JB.00684-06 )
• 2HRT: asymmetric structure of trimeric acrb from escherichia coli (10.1126/SCIENCE.1131542 )
• 2I6W: crystal structure of the multidrug efflux transporter acrb (10.1016/J.JSB.2006.12.004 )
• 2J8S: drug export pathway of multidrug exporter acrb revealed by darpin inhibitors (10.1371/JOURNAL.PBIO.0050007 )
• 2RDD: x-ray crystal structure of acrb in complex with a novel transmembrane helix. (10.1016/J.STR.2007.09.023 )
• 2W1B: the structure of the efflux pump acrb in complex with bile acid (10.1080/09687680802552257 )
• 3AOA: structures of the multidrug exporter acrb reveal a proximal multisite drug-binding pocket (10.1038/NATURE10641 )
• 3AOB: structures of the multidrug exporter acrb reveal a proximal multisite drug-binding pocket (10.1038/NATURE10641 )
• 3AOC: structures of the multidrug exporter acrb reveal a proximal multisite drug-binding pocket (10.1038/NATURE10641 )
• 3AOD: structures of the multidrug exporter acrb reveal a proximal multisite drug-binding pocket (10.1038/NATURE10641 )
• 3D9B: symmetric structure of e. coli acrb (10.1107/S1744309108028248 )
• 3NOC: designed ankyrin repeat protein (darpin) binders to acrb: plasticity of the interface (10.1016/J.JSB.2011.01.014 )
• 3NOG: designed ankyrin repeat protein (darpin) binders to acrb: plasticity of the interface (10.1016/J.JSB.2011.01.014 )
• 3W9H: structural basis for the inhibition of bacterial multidrug exporters (10.1038/NATURE12300 )
• 4C48: crystal structure of acrb-acrz complex (10.1038/NATURE13205 )
• 4CDI: crystal structure of acrb-acrz complex (10.1038/NATURE13205 )
• 4DX5: transport of drugs by the multidrug transporter acrb involves an access and a deep binding pocket that are separated by a switch-loop (10.1073/PNAS.1114944109 )
• 4DX6: transport of drugs by the multidrug transporter acrb involves an access and a deep binding pocket that are separated by a switch-loop (10.1073/PNAS.1114944109 )
• 4DX7: transport of drugs by the multidrug transporter acrb involves an access and a deep binding pocket that are separated by a switch-loop (10.1073/PNAS.1114944109 )
• 4K7Q: crystal structure of acrb complexed with linezolid at 3.5 resolution (10.1007/S10969-013-9154-X )
• 4U8V: coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump acrb (10.7554/ELIFE.03145 )
• 4U8Y: coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump acrb (10.7554/ELIFE.03145 )
• 4U95: coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump acrb (10.7554/ELIFE.03145 )
• 4U96: coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump acrb (10.7554/ELIFE.03145 )
• 4ZIT: crystal structure of acrb in p21 space group (10.1371/JOURNAL.PONE.0159154 )
• 4ZIV: crystal structure of acrb triple mutant in p21 space group (10.1371/JOURNAL.PONE.0159154 )
• 4ZIW: crystal structure of acrb deletion mutant in p21 space group (10.1371/JOURNAL.PONE.0159154 )
• 4ZJL: crystal structure of acrb in complex with antibiotic in p21 space group (10.1371/JOURNAL.PONE.0159154 )
• 4ZJO: crystal structure of acrb triple mutant in complex with antibiotic in p21 space group (10.1371/JOURNAL.PONE.0159154 )
• 4ZJQ: crystal structure of acrb deletion mutant in complex with antibiotic in p21 space group (10.1371/JOURNAL.PONE.0159154 )
• 4ZLJ: crystal structure of transporter acrb
• 4ZLL: crystal structure of transporter acrb triple mutant
• 4ZLN: crystal structure of transporter acrb deletion mutant
• 5EN5: apo structure of bacterial efflux pump. (10.1073/PNAS.1602472113 )
• 5ENO: mbx2319 bound structure of bacterial efflux pump. (10.1073/PNAS.1602472113 )
• 5ENP: mbx2931 bound structure of bacterial efflux pump. (10.1073/PNAS.1602472113 )
• 5ENQ: mbx3132 bound structure of bacterial efflux pump. (10.1073/PNAS.1602472113 )
• 5ENR: mbx3135 bound structure of bacterial efflux pump. (10.1073/PNAS.1602472113 )
• 5ENS: rhodamine bound structure of bacterial efflux pump. (10.1073/PNAS.1602472113 )
• 5ENT: minocycline bound structure of bacterial efflux pump. (10.1073/PNAS.1602472113 )
• 5JMN: fusidic acid bound acrb (10.1038/NCOMMS13819 )
• 5NC5: crystal structure of acrbz in complex with antibiotic puromycin (10.7554/ELIFE.24905 )
• 5NG5: multi-drug efflux; membrane transport; rnd superfamily; drug resistance (10.7554/ELIFE.24905 )
• 5O66: asymmetric acrabz-tolc (10.7554/ELIFE.24905 )
• 5V5S: multi-drug efflux; membrane transport; rnd superfamily; drug resistance (10.7554/ELIFE.24905 )
• 5YIL: hoisting-loop in bacterial multidrug exporter acrb is a highly flexible hinge that enables the large motion of the subdomains (10.3389/FMICB.2017.02095 )
• 6BAJ: cryo-em structure of lipid bilayer in the native cell membrane nanoparticles of acrb (10.1073/PNAS.1812526115 )
• 6CSX: single particles cryo-em structure of acrb d407a associated with lipid bilayer at 3.0 angstrom (10.1073/PNAS.1812526115 )
• 6NZI: low resolution crystal structure of the bacterial multidrug efflux transporter acrb in the presence of cadmium
• 6Q4N: fusidic acid bound acrb_v340a (10.1016/J.JMB.2019.12.025 )
• 6Q4O: fusidic acid bound acrb_i27a (10.1016/J.JMB.2019.12.025 )
• 6Q4P: fusidic acid bound acrb_n298a (10.1016/J.JMB.2019.12.025 )
• 6SGR: cryo-em structure of escherichia coli acrbz and darpin in saposin a- nanodisc with cardiolipin (10.1016/J.STR.2020.03.013 )
• 6SGS: cryo-em structure of escherichia coli acrbz and darpin in saposin a- nanodisc (10.1016/J.STR.2020.03.013 )
• 6SGT: cryo-em structure of escherichia coli acrb and darpin in saposin a- nanodisc with cardiolipin (10.1016/J.STR.2020.03.013 )
• 6SGU: cryo-em structure of escherichia coli acrb and darpin in saposin a- nanodisc (10.1016/J.STR.2020.03.013 )
• 6Z12: salmonella acrb solubilised in the sma copolymer (10.3390/MICROORGANISMS8060943 )
• 6ZO5: fusidic acid binding to the tm1/tm2 groove of acrb-g619p_g621p
• 6ZO6: minocycline binding to the deep binding pocket of acrb-g619p
• 6ZO7: 3-formylrifamycin sv binding to the access pocket of acrb-g619p l and t protomer
• 6ZO8: minocycline binding to the deep binding pocket of acrb-g621p
• 6ZO9: binding of two rifabutins to the access pocket of acrb-g621p t protomer
• 6ZOA: partially induced acrb t protomer and ddm binding to the tm8/pc2 pathway of acrb l2 protomer
• 6ZOB: 3-formylrifamycin sv binding to the access pocket of acrb l protomer
• 6ZOC: erythromycin binding to the access pocket of acrb-g616p l protomer and 3-formylrifamycin sv binding to the access pocket of acrb-g616p t protomer
• 6ZOD: fusidic acid binding to the allosteric deep transmembrane domain binding pocket, tm7/tm8 groove, and tm1/tm2 groove of the fully induced acrb t protomer
• 6ZOE: acrb-f563a symmetric t protomer
• 6ZOF: fusidic acid binding to the tm7/tm8 groove of acrb-f380a t protomer
• 6ZOG: minocycline binding to the deep binding pocket of acrb-i38f_i671t
• 6ZOH: 3-formylrifamycin sv binding to the access pocket of acrb-g619p_g621p l and t protomers