2vvz

X-ray diffraction
2.5Å resolution

Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA

Released:
Source organism: Streptococcus pneumoniae
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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158648 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 504 amino acids
Theoretical weight: 56.54 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P62575 (Residues: 319-822; Coverage: 51%)
Gene name: nanA
Sequence domains: BNR repeat-like domain
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 49.206Å b: 95.626Å c: 226.596Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 0.243 0.298
Expression system: Escherichia coli BL21(DE3)