PDBe 1w8n

X-ray diffraction
2.1Å resolution

Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens.


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
Sialidase Chain: A
Molecule details ›
Chain: A
Length: 601 amino acids
Theoretical weight: 64.24 KDa
Source organism: Micromonospora viridifaciens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q02834 (Residues: 47-647; Coverage: 99%)
Gene name: nedA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 46.602Å b: 111.608Å c: 143.865Å
α: 90° β: 90° γ: 90°
R R work R free
0.168 0.166 0.219
Expression system: Escherichia coli BL21(DE3)