› 2zml

X-ray diffraction
2.65Å resolution

Crystal structure of basic winged bean lectin in complex with Gal-ALPHA 1,4 Gal

Released:
DOI: 10.2210/pdb2zml/pdb
PDB entry 2zml coloured by chain, front view.
PDB entry 2zml coloured by chain, side view.
PDB entry 2zml coloured by chain, top view.
Source organism: Psophocarpus tetragonolobus
Primary publication:
Structure and sugar-specificity of basic winged-bean lectin: structures of new disaccharide complexes and a comparative study with other known disaccharide complexes of the lectin.
Kulkarni KA, Katiyar S, Surolia A, Vijayan M, Suguna K
Acta Crystallogr D Biol Crystallogr D64 730-7 (2008)
PMID: 18566508

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-127671 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Basic agglutinin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 241 amino acids
Theoretical weight: 26.51 KDa
Source organism: Psophocarpus tetragonolobus
UniProt:
  • Canonical: O24313 (Residues: 2-242; Coverage: 100%)
Gene name: WBAI
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLA
Carbohydrate polymer
3 bound ligands:
Ligand NAG 3 x NAG
Ligand MN 4 x MN
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21212
Unit cell:
a: 157.928Å b: 91.524Å c: 73.654Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.247

Quick links

Citations

2 review citations

The repertoire of glycan determinants in the human glycome.
Cummings RD. (2009)
1 more

1 mention without citation

Structural Diversities of Lectins Binding to the Glycosphingolipid Gb3.
Siukstaite et al. (2021)