› 5gze

X-ray diffraction
1.32Å resolution

Galectin-8 N-terminal domain carbohydrate recognition domain

Released:
DOI: 10.2210/pdb5gze/pdb
PDB entry 5gze coloured by chain, front view.
PDB entry 5gze coloured by chain, side view.
PDB entry 5gze coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker.
Si Y, Wang Y, Gao J, Song C, Feng S, Zhou Y, Tai G, Su J
OpenAccess logo Int J Mol Sci 17 (2016)
PMID: 27973456

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-517137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Galectin-8 Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00214 (Residues: 7-154; Coverage: 47%)
Gene name: LGALS8
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
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: C2
Unit cell:
a: 60.687Å b: 39.744Å c: 55.802Å
α: 90° β: 108.02° γ: 90°
R-values:
R R work R free
0.252 0.251 0.278
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Galectin Targeted Therapy in Oncology: Current Knowledge and Perspectives.
Wdowiak et al. (2018)
1 more

1 mention without citation

Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker.
Si et al. (2016)