› 5nf9

X-ray diffraction
1.87Å resolution

Structure of Galectin-3 CRD in complex with compound 2

Released:
DOI: 10.2210/pdb5nf9/pdb
PDB entry 5nf9 coloured by chain, front view.
PDB entry 5nf9 coloured by chain, side view.
PDB entry 5nf9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Biophysical and structural characterization of mono/di-arylated lactosamine derivatives interaction with human galectin-3.
Atmanene C, Ronin C, Téletchéa S, Gautier FM, Djedaïni-Pilard F, Ciesielski F, Vivat V, Grandjean C
Biochem Biophys Res Commun 489 281-286 (2017)
PMID: 28554839

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-538773 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galectin-3 Chain: A
Molecule details ›
Chain: A
Length: 147 amino acids
Theoretical weight: 16.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17931 (Residues: 106-250; Coverage: 58%)
Gene names: LGALS3, MAC2
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand 8VW 1 x 8VW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 36.87Å b: 57.95Å c: 62.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.148 0.145 0.214
Expression system: Escherichia coli

Quick links

Citations

1 review citation

π-Cation Interactions in Molecular Recognition: Perspectives on Pharmaceuticals and Pesticides.
Liang et al. (2018)
13 other articles

1 mention without citation

Computational Study of Potential Galectin-3 Inhibitors in the Treatment of COVID-19.
Aminpour et al. (2021)