› 6bpp

X-ray diffraction
2.92Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + lipid A-core oligosaccharide(Side 1) = ADP + phosphate + lipid A-core oligosaccharide(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-199680 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
ATP-dependent lipid A-core flippase Chains: A, B
Molecule details ›
Chains: A, B
Length: 582 amino acids
Theoretical weight: 64.49 KDa
Source organism: Escherichia coli CFT073
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8FJB1 (Residues: 2-582; Coverage: 100%)
Gene names: c1054, msbA
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: PA1, GCS, KDO, GMH, GLC
Carbohydrate polymer
6 bound ligands:
Ligand E1M 2 x E1M
Ligand FTT 4 x FTT
Ligand DAO 1 x DAO
Ligand 3PE 7 x 3PE
Ligand PO4 2 x PO4
Ligand MYR 1 x MYR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: C2
Unit cell:
a: 256.286Å b: 89.786Å c: 72.509Å
α: 90° β: 91.29° γ: 90°
R-values:
R R work R free
0.259 0.258 0.278
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Function and Biogenesis of Lipopolysaccharides.
Bertani et al. (2018)
26 more

6 mentions without citation

Structural and functional diversity calls for a new classification of ABC transporters.
Thomas et al. (2020)
5 more