PDBe 4fpe

X-ray diffraction
2.18Å resolution

Crystal structure of the NanB sialidase from streptococcus pneumoniae in complex with 2-[(4-Methoxybenzyl)ammonio]ethanesulfonate

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

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: 76.229Å b: 82.48Å c: 116.248Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.236
Expression system: Escherichia coli BL21(DE3)