1mv5

X-ray diffraction
3.1Å resolution

Crystal structure of LmrA ATP-binding domain

Released:
Source organism: Lactococcus lactis
Entry authors: Yuan Y, Chen H, Patel D

Function and Biology Details

Reaction catalysed:
ATP + H(2)O + xenobiotic(Side 1) = ADP + phosphate + xenobiotic(Side 2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-189968 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multidrug resistance ABC transporter ATP-binding and permease protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 243 amino acids
Theoretical weight: 26.89 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9CHL8 (Residues: 349-590; Coverage: 41%)
Gene names: L116532, LL0711, lmrA
Sequence domains: ABC transporter
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P63
Unit cell:
a: 141.866Å b: 141.866Å c: 120.965Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.251 0.283
Expression system: Escherichia coli BL21(DE3)