› 1wgc

X-ray diffraction
2.2Å resolution

2.2 ANGSTROMS RESOLUTION STRUCTURE ANALYSIS OF TWO REFINED N-ACETYLNEURAMINYLLACTOSE-WHEAT GERM AGGLUTININ ISOLECTIN COMPLEXES

Released:
DOI: 10.2210/pdb1wgc/pdb
PDB entry 1wgc coloured by chain, front view.
PDB entry 1wgc coloured by chain, side view.
PDB entry 1wgc coloured by chain, top view.
Source organism: Triticum aestivum
Primary publication:
2.2 A resolution structure analysis of two refined N-acetylneuraminyl-lactose--wheat germ agglutinin isolectin complexes.
Wright CS
J Mol Biol 215 635-51 (1990)
PMID: 2231724

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
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145543 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Agglutinin isolectin 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 171 amino acids
Theoretical weight: 17.12 KDa
Source organism: Triticum aestivum
Expression system: Not provided
UniProt:
  • Canonical: P10968 (Residues: 27-197; Coverage: 92%)
Sequence domains: Chitin recognition protein
Structure domains: Endochitinase-like

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GAL, SIA
Carbohydrate polymer
No bound ligands
1 modified residue:
Ligand PCA 2 x PCA

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 51Å b: 73.64Å c: 91.41Å
α: 90° β: 97.91° γ: 90°
R-values:
R R work R free
0.172 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Lectin-carbohydrate complexes of plants and animals: an atomic view.
Sharon N. (1993)
3 more

7 mentions without citation

Carbohydrate-binding modules: fine-tuning polysaccharide recognition.
Boraston et al. (2004)
6 more