PDBe 1w8o

X-ray diffraction
1.7Å resolution

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

Released:

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 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)
UniProt:
  • Canonical: Q02834 (Residues: 47-647; Coverage: 99%)
Gene name: nedA
Sequence domains:
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 46.712Å b: 111.168Å c: 142.195Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.197
Expression system: Escherichia coli BL21(DE3)