› 1kit

X-ray diffraction
2.3Å resolution

VIBRIO CHOLERAE NEURAMINIDASE

Released:
DOI: 10.2210/pdb1kit/pdb
PDB entry 1kit coloured by chain, front view.
PDB entry 1kit coloured by chain, side view.
PDB entry 1kit coloured by chain, top view.
Source organism: Vibrio cholerae
Primary publication:
Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain.
Crennell S, Garman E, Laver G, Vimr E, Taylor G
Structure 2 535-44 (1994)
PMID: 7922030

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-143046 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase Chain: A
Molecule details ›
Chain: A
Length: 757 amino acids
Theoretical weight: 83.04 KDa
Source organism: Vibrio cholerae
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C6E9 (Residues: 25-781; Coverage: 100%)
Gene names: VC_1784, nanH
Sequence domains: Vibrio cholerae sialidase, lectin insertion
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 72.3Å b: 78.9Å c: 164.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 not available
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Diversity of microbial sialic acid metabolism.
Vimr et al. (2004)
17 more

11 mentions without citation

Unraveling virus relationships by structure-based phylogenetic classification.
Ng et al. (2020)
10 more