PDBe 2vk7

X-ray diffraction
1.2Å resolution

THE STRUCTURE OF CLOSTRIDIUM PERFRINGENS NANI SIALIDASE AND ITS CATALYTIC INTERMEDIATES

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. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exo-alpha-sialidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 452 amino acids
Theoretical weight: 50.41 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59310 (Residues: 243-694; Coverage: 65%)
Gene name: nanH
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: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 69.6Å b: 97.4Å c: 72.6Å
α: 90° β: 91° γ: 90°
R-values:
R R work R free
0.132 0.131 0.159
Expression system: Escherichia coli