› 1vcu

X-ray diffraction
2.85Å resolution

Structure of the human cytosolic sialidase Neu2 in complex with the inhibitor DANA

Released:
DOI: 10.2210/pdb1vcu/pdb
PDB entry 1vcu coloured by chain, front view.
PDB entry 1vcu coloured by chain, side view.
PDB entry 1vcu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition.
Chavas LM, Tringali C, Fusi P, Venerando B, Tettamanti G, Kato R, Monti E, Wakatsuki S
J Biol Chem 280 469-75 (2005)
PMID: 15501818

Function and Biology Details

Reaction catalysed: 
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195217 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 382 amino acids
Theoretical weight: 42.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9Y3R4 (Residues: 1-380; Coverage: 100%)
Gene name: NEU2
Sequence domains: BNR repeat-like domain
Structure domains: Neuraminidase

Ligands and Environments

2 bound ligands:
Ligand DAN 2 x DAN
Ligand EPE 4 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2
Unit cell:
a: 157.65Å b: 74Å c: 77.19Å
α: 90° β: 90.64° γ: 90°
R-values:
R R work R free
0.199 0.195 0.266
Expression system: Escherichia coli BL21

Quick links

Citations

15 review citations

Sialic acids as regulators of molecular and cellular interactions.
Schauer R. (2009)
14 more

15 mentions without citation

Sialidase and Sialyltransferase Inhibitors: Targeting Pathogenicity and Disease.
Bowles et al. (2021)
14 more