› 1dbn

X-ray diffraction
2.75Å resolution

MAACKIA AMURENSIS LEUKOAGGLUTININ (LECTIN) WITH SIALYLLACTOSE

Released:
DOI: 10.2210/pdb1dbn/pdb
PDB entry 1dbn coloured by chain, front view.
PDB entry 1dbn coloured by chain, side view.
PDB entry 1dbn coloured by chain, top view.
Source organism: Maackia amurensis
Primary publication:
An unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharides.
Imberty A, Gautier C, Lescar J, Pérez S, Wyns L, Loris R
J Biol Chem 275 17541-8 (2000)
PMID: 10747930

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161074 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Bark leucoagglutinin Chains: A, B
Molecule details ›
Chains: A, B
Length: 239 amino acids
Theoretical weight: 25.99 KDa
Source organism: Maackia amurensis
UniProt:
  • Canonical: P93248 (Residues: 29-267; Coverage: 93%)
Gene name: MAL
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GAL, SIA
Carbohydrate polymer
3 bound ligands:
Ligand NAG 5 x NAG
Ligand CA 2 x CA
Ligand MN 2 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21212
Unit cell:
a: 80.742Å b: 88.45Å c: 84.496Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.253

Quick links

Citations

9 review citations

Diversity in cell surface sialic acid presentations: implications for biology and disease.
Varki et al. (2007)
8 more

11 mentions without citation

Research advances and prospects of legume lectins.
Katoch et al. (2021)
10 more