PDBe 2f12

X-ray diffraction
2.27Å resolution

Crystal Structure of the Human Sialidase Neu2 in Complex with 3- hydroxypropyl ether mimetic Inhibitor

Released:
Source organism: Homo sapiens
Entry authors: Chavas LMG, Kato R, Mann MC, Thomson RJ, Dyason JC, von Itzstein M, Fusi P, Tringali C, Venerando B, Tettamanti G, Monti E, Wakatsuki S

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. 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2221
Unit cell:
a: 87.59Å b: 87.97Å c: 92.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.25
Expression system: Escherichia coli BL21