› 5h9p

X-ray diffraction
2.04Å resolution

Crystal Structure of Human Galectin-3 CRD in Complex with TD139

Released:
DOI: 10.2210/pdb5h9p/pdb
PDB entry 5h9p coloured by chain, front view.
PDB entry 5h9p coloured by chain, side view.
PDB entry 5h9p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Dual thio-digalactoside-binding modes of human galectins as the structural basis for the design of potent and selective inhibitors.
Hsieh TJ, Lin HY, Tu Z, Lin TC, Wu SC, Tseng YY, Liu FT, Hsu ST, Lin CH
OpenAccess logo Sci Rep 6 29457 (2016)
PMID: 27416897

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: 158 amino acids
Theoretical weight: 17.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P17931 (Residues: 113-250; Coverage: 55%)
Gene names: LGALS3, MAC2
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand TD2 1 x TD2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 37.168Å b: 57.145Å c: 63.651Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.165 0.195
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

8 review citations

Galectin-3: One Molecule for an Alphabet of Diseases, from A to Z.
Sciacchitano et al. (2018)
7 more

9 mentions without citation

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