› 1axy

X-ray diffraction
1.95Å resolution

ERYTHRINA CORALLODENDRON LECTIN

Released:
DOI: 10.2210/pdb1axy/pdb
PDB entry 1axy coloured by chain, front view.
PDB entry 1axy coloured by chain, side view.
PDB entry 1axy coloured by chain, top view.
Source organism: Erythrina corallodendron
Primary publication:
Structures of the Erythrina corallodendron lectin and of its complexes with mono- and disaccharides.
Elgavish S, Shaanan B
J Mol Biol 277 917-32 (1998)
PMID: 9545381

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-147701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lectin Chain: A
Molecule details ›
Chain: A
Length: 239 amino acids
Theoretical weight: 26.22 KDa
Source organism: Erythrina corallodendron
UniProt:
  • Canonical: P16404 (Residues: 27-265; Coverage: 94%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, XYP, MAN, FUC
Carbohydrate polymer
2 bound ligands:
Ligand MN 1 x MN
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 84.605Å b: 72.881Å c: 71.338Å
α: 90° β: 113.48° γ: 90°
R-values:
R R work R free
0.177 0.177 0.2

Quick links

Citations

9 review citations

Cross-reactivity of IgE antibodies to allergens.
Aalberse et al. (2001)
8 more

7 mentions without citation

Insights into the quaternary association of proteins through structure graphs: a case study of lectins.
Brinda et al. (2005)
6 more