› 1lu1

X-ray diffraction
2.6Å resolution

THE STRUCTURE OF THE DOLICHOS BIFLORUS SEED LECTIN IN COMPLEX WITH THE FORSSMAN DISACCHARIDE

Released:
DOI: 10.2210/pdb1lu1/pdb
PDB entry 1lu1 coloured by chain, front view.
PDB entry 1lu1 coloured by chain, side view.
PDB entry 1lu1 coloured by chain, top view.
Source organism: Vigna unguiculata subsp. cylindrica
Primary publication:
Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus.
Hamelryck TW, Loris R, Bouckaert J, Dao-Thi MH, Strecker G, Imberty A, Fernandez E, Wyns L, Etzler ME
J Mol Biol 286 1161-77 (1999)
PMID: 10047489

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138337 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Seed lectin subunit I Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 27.12 KDa
Source organism: Vigna unguiculata subsp. cylindrica
Expression system: Escherichia coli
UniProt:
  • Canonical: P05045 (Residues: 23-275; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: NGA, A2G
Carbohydrate polymer
3 bound ligands:
Ligand CA 1 x CA
Ligand MN 1 x MN
Ligand ADE 1 x ADE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I4122
Unit cell:
a: 79.05Å b: 79.05Å c: 260.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.234
Expression system: Escherichia coli

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Citations

7 review citations

Lectins.
Vijayan et al. (1999)
6 more

7 mentions without citation

Are Dietary Lectins Relevant Allergens in Plant Food Allergy?
Barre et al. (2020)
6 more