PDBe 2w20

X-ray diffraction
1.49Å resolution

Structure of the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae

Released:
Source organism: Streptococcus pneumoniae R6
Primary publication:
Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA.
OpenAccess logo Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 772-5 (2008)
PMID: 18765901

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:
Sialidase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 471 amino acids
Theoretical weight: 52.95 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P62576 (Residues: 321-791; Coverage: 48%)
Gene names: nanA, spr1536
Sequence domains: BNR/Asp-box repeat
Structure domains: Neuraminidase

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 47.2Å b: 96.6Å c: 218.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.2 0.225
Expression system: Escherichia coli BL21(DE3)