› 6mbn

X-ray diffraction
1.96Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141929 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipopolysaccharide export system ATP-binding protein LptB Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 26.79 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli KRX
UniProt:
  • Canonical: P0A9V1 (Residues: 2-241; Coverage: 100%)
Gene names: JW3168, b3201, lptB, yhbG
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand NA 2 x NA
Ligand ATP 2 x ATP
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2221
Unit cell:
a: 65.351Å b: 137.585Å c: 100.971Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.219
Expression system: Escherichia coli KRX

Quick links

Citations

4 review citations

Assembly and Maintenance of Lipids at the Bacterial Outer Membrane.
Lundstedt et al. (2021)
3 more

4 mentions without citation

Combining Mutations That Inhibit Two Distinct Steps of the ATP Hydrolysis Cycle Restores Wild-Type Function in the Lipopolysaccharide Transporter and Shows that ATP Binding Triggers Transport.
Simpson et al. (2019)
3 more