2gif » Multidrug efflux transporter AcrB, asymmetric 1
- Type: Transmembrane (3 classes)
- Class: Alpha-helical polytopic (156 superfamilies)
- Superfamily: Resistance-nodulation-cell division (5 families) 2.A.6 (TCDB) CL0322
- Family: Hydrophobe/amphiphile efflux-1 family (52 proteins) 2.A.6.2 (TCDB) PF00873 IPR004764 PDBsum
- Species: Escherichia coli (636 proteins)
- Localization: Bacterial Gram-negative inner membrane (1251 proteins)
2gif >> Multidrug efflux transporter AcrB, asymmetric 1 | |
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Hydrophobic Thickness or Depth | 29.0 Å |
Tilt Angle | 1° |
ΔGtransfer | -187.5 kcal/mol |
Links to 2gif | PDB Sum, PDB, MSD, MMDB, Encompass |
Topology | subunit A (N terminus cytoplasmic side) |
Resolution | 2.9 |
Primary PDB represention | 2gif |
Other PDB entries representing this structure | 2dhh (2.8), 2dr6 (3.3), 2drd (3.1), 2hrt (3.0), 3aoa (3.35), 3aob (3.35), 3aoc (3.34), 3aod (3.3), 3w9h (3.05), 4zit (3.3), 4ziv (3.16), 4ziw (3.4), 4zjl (3.47), 4zjo (3.6), 4zjq (3.59), 5jmn (2.5), 5yil (3.0), 6q4n (2.8), 6q4o (2.8), 6q4p (2.8) |
Number of TM secondary structures | 36 |
Membranome | ![]() |
Uniprot | ACRB_ECOLI |
Comments: Residues 499-515 are ordered in 2gif and 2hrt but disordered in all other structures of AcrB. Three subunits are not identical. Therefore, their tilt angles and some transmembrane segments are slightly different. The substrate is bound to the stronger tilted subunit B.
Subunits: 3 | |||
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A - Tilt: 2 - TM segments: 1(10-27),2(340-358),3(363-386),4(395-414),5(438-457),6(470-493),7(539-556),8(873-892),9(896-918),10(927-947),11(971-991),12(1003-1026) | |||
B - Tilt: 6 - TM segments: 1(10-27),2(340-358),3(363-383),4(397-414),5(438-456),6(471-493),7(539-556),8(874-892),9(896-918),10(927-947),11(971-991),12(1003-1026) | |||
C - Tilt: 3 - TM segments: 1(10-27),2(340-358),3(363-386),4(394-413),5(439-457),6(470-492),7(539-557),8(873-892),9(896-918),10(927-947),11(972-991),12(1002-1025) |