› 1dim

X-ray diffraction
1.6Å resolution

SIALIDASE FROM SALMONELLA TYPHIMURIUM COMPLEXED WITH EPANA INHIBITOR

Released:
DOI: 10.2210/pdb1dim/pdb
PDB entry 1dim coloured by chain, front view.
PDB entry 1dim coloured by chain, side view.
PDB entry 1dim coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Primary publication:
The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution.
Crennell SJ, Garman EF, Philippon C, Vasella A, Laver WG, Vimr ER, Taylor GL
J Mol Biol 259 264-80 (1996)
PMID: 8656428

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151572 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase Chain: A
Molecule details ›
Chain: A
Length: 381 amino acids
Theoretical weight: 41.99 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli
UniProt:
  • Canonical: P29768 (Residues: 2-382; Coverage: 100%)
Gene names: STM0928, nanH
Structure domains: Neuraminidase

Ligands and Environments

2 bound ligands:
Ligand K 1 x K
Ligand EQP 1 x EQP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 47.4Å b: 82.3Å c: 91.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Structural and sequence-based classification of glycoside hydrolases.
Henrissat et al. (1997)
7 more

9 mentions without citation

Sialidases from gut bacteria: a mini-review.
Juge et al. (2016)
8 more