› 1slt

X-ray diffraction
1.9Å resolution

STRUCTURE OF S-LECTIN, A DEVELOPMENTALLY REGULATED VERTEBRATE BETA-GALACTOSIDE BINDING PROTEIN

Released:
DOI: 10.2210/pdb1slt/pdb
PDB entry 1slt coloured by chain, front view.
PDB entry 1slt coloured by chain, side view.
PDB entry 1slt coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein.
Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O
Proc Natl Acad Sci U S A 91 1428-32 (1994)
PMID: 8108426

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145658 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Galectin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 134 amino acids
Theoretical weight: 14.77 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P11116 (Residues: 2-135; Coverage: 99%)
Gene name: LGALS1
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: NDG, GAL
Carbohydrate polymer
1 bound ligand:
Ligand CL 1 x CL
1 modified residue:
Ligand OCS 6 x OCS

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 59.3Å b: 62.9Å c: 70.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.167 not available
Expression system: Not provided

Quick links

Citations

36 review citations

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

19 mentions without citation

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