PDBe 2vnv

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

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lectin 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)
UniProt:
  • 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-values:
R R work R free
0.171 0.169 0.203
Expression system: Escherichia coli BL21(DE3)