› 1w8n

X-ray diffraction
2.1Å resolution

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

Released:
DOI: 10.2210/pdb1w8n/pdb
PDB entry 1w8n coloured by chain, front view.
PDB entry 1w8n coloured by chain, side view.
PDB entry 1w8n coloured by chain, top view.
Source organism: Micromonospora viridifaciens
Primary publication:
Contribution of the active site aspartic acid to catalysis in the bacterial neuraminidase from Micromonospora viridifaciens.
Watson JN, Newstead S, Dookhun V, Taylor G, Bennet AJ
FEBS Lett 577 265-9 (2004)
PMID: 15527797

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169775 (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

3 bound ligands:
Ligand GAL 1 x GAL
Ligand DAN 1 x DAN
Ligand NA 1 x NA
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-values:
R R work R free
0.168 0.166 0.219
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Features and applications of bacterial sialidases.
Kim et al. (2011)
8 other articles

2 mentions without citation

Automated identification of protein-ligand interaction features using Inductive Logic Programming: a hexose binding case study.
A Santos et al. (2012)
1 more