› 4i4q

X-ray diffraction
1.51Å resolution

BEL beta-trefoil apo crystal form 3

Released:
DOI: 10.2210/pdb4i4q/pdb
PDB entry 4i4q coloured by chain, front view.
PDB entry 4i4q coloured by chain, side view.
PDB entry 4i4q coloured by chain, top view.
Source organism: Boletus edulis
Primary publication:
BEL β-trefoil: a novel lectin with antineoplastic properties in king bolete (Boletus edulis) mushrooms.
Bovi M, Cenci L, Perduca M, Capaldi S, Carrizo ME, Civiero L, Chiarelli LR, Galliano M, Monaco HL
Glycobiology 23 578-92 (2013)
PMID: 23213111

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195739 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BEL-beta trefoil Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 16.59 KDa
Source organism: Boletus edulis
UniProt:
  • Canonical: R4GRU4 (Residues: 1-146; Coverage: 100%)
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

1 bound ligand:
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P3221
Unit cell:
a: 77.744Å b: 77.744Å c: 52.772Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.188 0.215

Quick links

Citations

6 review citations

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

1 mention without citation

Mushroom lectins: specificity, structure and bioactivity relevant to human disease.
Hassan et al. (2015)