› 3vkn

X-ray diffraction
1.98Å resolution

Galectin-8 N-terminal domain in free form

Released:
DOI: 10.2210/pdb3vkn/pdb
PDB entry 3vkn coloured by chain, front view.
PDB entry 3vkn coloured by chain, side view.
PDB entry 3vkn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
X-ray structure of a protease-resistant mutant form of human galectin-8 with two carbohydrate recognition domains.
Yoshida H, Yamashita S, Teraoka M, Itoh A, Nakakita S, Nishi N, Kamitori S
FEBS J 279 3937-51 (2012)
PMID: 22913484

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-126160 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galectin-8 Chains: A, B
Molecule details ›
Chains: A, B
Length: 153 amino acids
Theoretical weight: 17.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00214 (Residues: 1-153; Coverage: 48%)
Gene name: LGALS8
Sequence domains: Galactoside-binding lectin
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 54.61Å b: 62.47Å c: 80.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.251
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Galectin-8: a matricellular lectin with key roles in angiogenesis.
Troncoso et al. (2014)
4 more

2 mentions without citation

Lactose Binding Induces Opposing Dynamics Changes in Human Galectins Revealed by NMR-Based Hydrogen-Deuterium Exchange.
Chien et al. (2017)
1 more