› 4nc5

X-ray diffraction
2.51Å resolution

Human sialidase 2 in complex with 2,3-difluorosialic acid (covalent intermediate)

Released:
DOI: 10.2210/pdb4nc5/pdb
PDB entry 4nc5 coloured by chain, front view.
PDB entry 4nc5 coloured by chain, side view.
PDB entry 4nc5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Tuning mechanism-based inactivators of neuraminidases: mechanistic and structural insights.
Buchini S, Gallat FX, Greig IR, Kim JH, Wakatsuki S, Chavas LM, Withers SG
Angew Chem Int Ed Engl 53 3382-6 (2014)
PMID: 24591206

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195217 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase-2 Chain: A
Molecule details ›
Chain: A
Length: 382 amino acids
Theoretical weight: 42.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y3R4 (Residues: 1-380; Coverage: 100%)
Gene name: NEU2
Sequence domains: BNR repeat-like domain
Structure domains: Neuraminidase

Ligands and Environments

2 bound ligands:
Ligand FSI 1 x FSI
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2221
Unit cell:
a: 87.408Å b: 87.916Å c: 92.394Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.174 0.263
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Sialidase Inhibitors with Different Mechanisms.
Keil et al. (2022)
2 more