3zw0

X-ray diffraction
1.6Å resolution

Structure of BambL lectin from Burkholderia ambifaria

Released:
Source organism: Burkholderia ambifaria AMMD
Entry authors: Audfray A, Claudinon J, Abounit S, Ruvoen-Clouet N, Larson G, Wimmerova M, LePendu J, Romer W, Varrot A, Imberty A

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fucose-binding lectin protein Chains: A, C
Molecule details ›
Chains: A, C
Length: 87 amino acids
Theoretical weight: 9.39 KDa
Source organism: Burkholderia ambifaria AMMD
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q0B4G1 (Residues: 1-87; Coverage: 100%)
Gene names: Bamb_5415, CH72_5454, rsl
Sequence domains: Fungal fucose-specific lectin
Structure domains: Lipocalin
Fucose-binding lectin protein Chain: B
Molecule details ›
Chain: B
Length: 87 amino acids
Theoretical weight: 9.4 KDa
Source organism: Burkholderia ambifaria AMMD
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q0B4G1 (Residues: 1-87; Coverage: 100%)
Gene names: Bamb_5415, CH72_5454, rsl
Sequence domains: Fungal fucose-specific lectin
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 45.11Å b: 47.25Å c: 98.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.146 0.143 0.188
Expression system: Escherichia coli BL21(DE3)