› 3t2t

X-ray diffraction
1.9Å resolution

Crystal structure of human galectin-1 in complex with methyl 2-O-acetyl-3-O-toluoyl-beta-D-talopyranoside

Released:
DOI: 10.2210/pdb3t2t/pdb
PDB entry 3t2t coloured by chain, front view.
PDB entry 3t2t coloured by chain, side view.
PDB entry 3t2t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Taloside inhibitors of galectin-1 and galectin-3.
Collins PM, Oberg CT, Leffler H, Nilsson UJ, Blanchard H
Chem Biol Drug Des 79 339-46 (2012)
PMID: 22136701

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140624 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galectin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 135 amino acids
Theoretical weight: 14.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09382 (Residues: 1-135; Coverage: 100%)
Gene name: LGALS1
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand MQT 1 x MQT
1 modified residue:
Ligand CME 6 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P212121
Unit cell:
a: 44.687Å b: 58.444Å c: 112.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.188 0.226
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Galectin-1 as a potent target for cancer therapy: role in the tumor microenvironment.
Ito et al. (2012)
8 more

3 mentions without citation

The Structural Biology of Galectin-Ligand Recognition: Current Advances in Modeling Tools, Protein Engineering, and Inhibitor Design.
Modenutti et al. (2019)
2 more