X-ray diffraction
1.7Å resolution

Crystal structure of BclA lectin from burkholderia cenocepacia in complex with alpha-methyl-mannoside at 1.7 Angstrom resolution


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-110046 (preferred)
Entry contents:
1 distinct polypeptide molecule
Calcium-mediated lectin domain-containing protein Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 129 amino acids
Theoretical weight: 13.91 KDa
Source organism: Burkholderia cenocepacia J2315
Expression system: Escherichia coli BL21(DE3)
  • Canonical: B4EH87 (Residues: 1-129; Coverage: 100%)
Gene name: BCAM0186
Sequence domains: Fucose-binding lectin II (PA-IIL)
Structure domains: Calcium-mediated lectin

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: C2221
Unit cell:
a: 50.01Å b: 185.702Å c: 187.551Å
α: 90° β: 90° γ: 90°
R R work R free
0.171 0.169 0.203
Expression system: Escherichia coli BL21(DE3)