› 5exo

X-ray diffraction
1.5Å resolution

Crystal structure of Human galectin-3 CRD in complex with methyl 2-O-acetyl-3-O-(2H-chromene-3-yl-methyl)-a-D-galactopyranoside inhibitor

Released:
DOI: 10.2210/pdb5exo/pdb
PDB entry 5exo coloured by chain, front view.
PDB entry 5exo coloured by chain, side view.
PDB entry 5exo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A Selective Galactose-Coumarin-Derived Galectin-3 Inhibitor Demonstrates Involvement of Galectin-3-glycan Interactions in a Pulmonary Fibrosis Model.
Rajput VK, MacKinnon A, Mandal S, Collins P, Blanchard H, Leffler H, Sethi T, Schambye H, Mukhopadhyay B, Nilsson UJ
J Med Chem 59 8141-7 (2016)
PMID: 27500311

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-148215 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galectin-3 Chain: A
Molecule details ›
Chain: A
Length: 139 amino acids
Theoretical weight: 15.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P17931 (Residues: 112-250; Coverage: 56%)
Gene names: LGALS3, MAC2
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand CL 1 x CL
Ligand 5SY 1 x 5SY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P212121
Unit cell:
a: 36.796Å b: 58.411Å c: 63.928Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.157 0.193
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Galectins at a glance.
Johannes et al. (2018)
8 more

3 mentions without citation

Binding of Gold(III) Porphyrin by the Pro-metastatic Regulatory Protein Human Galectin-3.
Bogoeva et al. (2019)
2 more