› 2x2t

X-ray diffraction
1.97Å resolution

CRYSTAL STRUCTURE OF SCLEROTINIA SCLEROTIORUM AGGLUTININ SSA in complex with Gal-beta1,3-Galnac

Released:
DOI: 10.2210/pdb2x2t/pdb
PDB entry 2x2t coloured by chain, front view.
PDB entry 2x2t coloured by chain, side view.
PDB entry 2x2t coloured by chain, top view.
Source organism: Sclerotinia sclerotiorum
Primary publication:
Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain.
Sulzenbacher G, Roig-Zamboni V, Peumans WJ, Rougé P, Van Damme EJ, Bourne Y
J Mol Biol 400 715-23 (2010)
PMID: 20566411

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108483 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Agglutinin Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 16.76 KDa
Source organism: Sclerotinia sclerotiorum
UniProt:
  • Canonical: A7XUK7 (Residues: 1-153; Coverage: 100%)
Sequence domains: Ricin-type beta-trefoil lectin domain-like
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

Carbohydrate polymer : NEW Components: NGA, GAL
Carbohydrate polymer
2 bound ligands:
Ligand SO4 4 x SO4
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P6122
Unit cell:
a: 51.458Å b: 51.458Å c: 295.987Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.163 0.195

Quick links

Citations

4 review citations

Fungal lectins: structure, function and potential applications.
Varrot et al. (2013)
3 more

3 mentions without citation

Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain.
Sulzenbacher et al. (2010)
2 more