› 5dg2

X-ray diffraction
1.61Å resolution

Sugar binding protein - human galectin-2 (dimer)

Released:
DOI: 10.2210/pdb5dg2/pdb
PDB entry 5dg2 coloured by chain, front view.
PDB entry 5dg2 coloured by chain, side view.
PDB entry 5dg2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human galectin-2 interacts with carbohydrates and peptides non-classically: new insight from X-ray crystallography and hemagglutination.
Si Y, Feng S, Gao J, Wang Y, Zhang Z, Meng Y, Zhou Y, Tai G, Su J
Acta Biochim Biophys Sin (Shanghai) 48 939-947 (2016)
PMID: 27563008

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-138568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Galectin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 135 amino acids
Theoretical weight: 14.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05162 (Residues: 1-132; Coverage: 100%)
Gene name: LGALS2
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, GAL
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Unit cell:
a: 38.06Å b: 66.08Å c: 106.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.234
Expression system: Escherichia coli

Quick links

Citations

3 review citations

A Brief History of Charcot-Leyden Crystal Protein/Galectin-10 Research.
Su J. (2018)
2 more

2 mentions without citation

Glycomimetics for the inhibition and modulation of lectins.
Leusmann et al. (2023)
1 more