X-ray diffraction
3.3Å resolution

Crystal structure of AcrB-AcrZ complex


Function and Biology Details

Structure analysis Details

Assembly composition:
hetero nonamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Multidrug efflux pump subunit AcrB Chain: A
Molecule details ›
Chain: A
Length: 1047 amino acids
Theoretical weight: 113.39 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P31224 (Residues: 1-1047; Coverage: 100%)
Gene names: JW0451, acrB, acrE, b0462
Sequence domains: AcrB/AcrD/AcrF family
Structure domains:
Molecule details ›
Chain: B
Length: 169 amino acids
Theoretical weight: 18.32 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
Structure domains: Ankyrin repeat-containing domain
Multidrug efflux pump accessory protein AcrZ Chain: C
Molecule details ›
Chain: C
Length: 49 amino acids
Theoretical weight: 5.3 KDa
Source organism: Escherichia coli str. K-12 substr. W3110
Expression system: Escherichia coli K-12
  • Canonical: P0AAW9 (Residues: 1-49; Coverage: 100%)
Gene names: JW5102, acrZ, b0762, ybhT
Sequence domains: Multidrug efflux pump-associated protein AcrZ
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: R32
Unit cell:
a: 145.01Å b: 145.01Å c: 538.34Å
α: 90° β: 90° γ: 120°
R R work R free
0.283 0.281 0.322
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli K-12