PDBe 2vw0

X-ray diffraction
2.3Å resolution

Crystal structure of the NanB sialidase from Streptococcus pneumoniae

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase B Chain: A
Molecule details ›
Chain: A
Length: 697 amino acids
Theoretical weight: 77.78 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q54727 (Residues: 1-697; Coverage: 100%)
Gene names: SP_1687, nanB
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 77.36Å b: 83.417Å c: 120.149Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.172 0.232
Expression system: Escherichia coli BL21(DE3)