› 1hlc

X-ray diffraction
2.9Å resolution

X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1hlc/pdb
PDB entry 1hlc coloured by chain, front view.
PDB entry 1hlc coloured by chain, side view.
PDB entry 1hlc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.
Lobsanov YD, Gitt MA, Leffler H, Barondes SH, Rini JM
J Biol Chem 268 27034-8 (1993)
PMID: 8262940

Function and Biology Details

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

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: 129 amino acids
Theoretical weight: 14.37 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05162 (Residues: 4-132; Coverage: 98%)
Gene name: LGALS2
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 43.6Å b: 57.8Å c: 108.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 not available
Expression system: Not provided

Quick links

Citations

39 review citations

Galectins: structure, function and therapeutic potential.
Yang et al. (2008)
38 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