X-ray diffraction
2.2Å resolution

Crystal structure of OpuAC from B. subtilis in complex with Arsenobetaine


Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Glycine betaine-binding protein OpuAC Chains: C, D
Molecule details ›
Chains: C, D
Length: 268 amino acids
Theoretical weight: 29.78 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
  • Canonical: P46922 (Residues: 26-293; Coverage: 98%)
Gene names: BSU03000, opuAC
Sequence domains: Substrate binding domain of ABC-type glycine betaine transport system
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 88.1Å b: 30Å c: 106.1Å
α: 90° β: 95.6° γ: 90°
R R work R free
0.188 0.184 0.282
Expression system: Escherichia coli