› 1so7

X-ray diffraction
1.49Å resolution

Maltose-induced structure of the human cytolsolic sialidase Neu2

Released:
DOI: 10.2210/pdb1so7/pdb
PDB entry 1so7 coloured by chain, front view.
PDB entry 1so7 coloured by chain, side view.
PDB entry 1so7 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 Chain: A
Molecule details ›
Chain: A
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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: R3
Unit cell:
a: 145.69Å b: 145.69Å c: 64.38Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.202 0.213
Expression system: Escherichia coli BL21

Quick links

Citations

16 review citations

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

4 mentions without citation

Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families.
Quistgaard et al. (2009)
3 more