› 3aya

X-ray diffraction
2Å resolution

Crystal structure of galectin-3 CRD domian complexed with Thomsen-Friedenreich antigen

Released:
DOI: 10.2210/pdb3aya/pdb
PDB entry 3aya coloured by chain, front view.
PDB entry 3aya coloured by chain, side view.
PDB entry 3aya coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for distinct binding properties of the human galectins to Thomsen-Friedenreich antigen.
Bian CF, Zhang Y, Sun H, Li DF, Wang DC
PLoS One 6 e25007 (2011)
PMID: 21949831

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
Macromolecules (2 distinct):
Galectin-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 135 amino acids
Theoretical weight: 15.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17931 (Residues: 117-250; Coverage: 54%)
Gene names: LGALS3, MAC2
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: A2G, GAL
Carbohydrate polymer
2 bound ligands:
Ligand THR 2 x THR
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 32.72Å b: 51.33Å c: 59.77Å
α: 64.7° β: 85.33° γ: 80.33°
R-values:
R R work R free
0.199 0.199 0.238
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Role of protein glycosylation in cancer metastasis.
Oliveira-Ferrer et al. (2017)
10 more

3 mentions without citation

Interaction of the Oncofetal Thomsen-Friedenreich Antigen with Galectins in Cancer Progression and Metastasis.
Sindrewicz et al. (2016)
2 more