› 6a1v

X-ray diffraction
1.98Å resolution

Charcot-Leyden crystal protein/Galectin-10 variant E33Q

Released:
DOI: 10.2210/pdb6a1v/pdb
PDB entry 6a1v coloured by chain, front view.
PDB entry 6a1v coloured by chain, side view.
PDB entry 6a1v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Identification of key amino acid residues determining ligand binding specificity, homodimerization and cellular distribution of human galectin-10.
Su J, Song C, Si Y, Cui L, Yang T, Li Y, Wang H, Tai G, Zhou Y
Glycobiology 29 85-93 (2019)
PMID: 30239701

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-170169 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galectin-10 Chain: A
Molecule details ›
Chain: A
Length: 145 amino acids
Theoretical weight: 16.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05315 (Residues: 1-142; Coverage: 100%)
Gene names: CLC, LGALS10, LGALS10A
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P6522
Unit cell:
a: 48.967Å b: 48.967Å c: 259.759Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.199 0.232
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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