› 1oyd

X-ray diffraction
3.8Å resolution

Structural Basis of Multiple Binding Capacity of the AcrB multidrug Efflux Pump

Released:
DOI: 10.2210/pdb1oyd/pdb
PDB entry 1oyd coloured by chain, front view.
PDB entry 1oyd coloured by chain, side view.
PDB entry 1oyd coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump.
Yu EW, McDermott G, Zgurskaya HI, Nikaido H, Koshland DE
Science 300 976-80 (2003)
PMID: 12738864

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151927 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multidrug efflux pump subunit AcrB Chain: A
Molecule details ›
Chain: A
Length: 1049 amino acids
Theoretical weight: 113.67 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P31224 (Residues: 1-1049; Coverage: 100%)
Gene names: JW0451, acrB, acrE, b0462
Sequence domains: AcrB/AcrD/AcrF family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand DEQ 1 x DEQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: R32
Unit cell:
a: 144.767Å b: 144.767Å c: 517.891Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.287 0.284 0.338
Expression system: Escherichia coli

Quick links

Citations

77 review citations

Molecular basis of bacterial outer membrane permeability revisited.
Nikaido H. (2003)
76 more

3 mentions without citation

Structural Insights into Transporter-Mediated Drug Resistance in Infectious Diseases.
Kim et al. (2021)
2 more