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PDBsum entry 4fov

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protein ligands links
Hydrolase/inhibitor PDB id
4fov
Jmol
Contents
Protein chain
658 a.a.
Ligands
CXS
DMS ×2
Waters ×503
PDB id:
4fov
Name: Hydrolase/inhibitor
Title: Crystal structure of the nanb sialidase from streptococcus p in complex with 3-cyclohexyl-1-propylsulfonic acid
Structure: Sialidase b. Chain: a. Synonym: neuraminidase b. Engineered: yes
Source: Streptococcus pneumoniae. Organism_taxid: 1313. Strain: tigr4. Gene: nanb, sp_1687. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.29Å     R-factor:   0.182     R-free:   0.234
Authors: P.Brear
Key ref: P.Brear et al. (2012). Synthesis and structural characterisation of selective non-carbohydrate-based inhibitors of bacterial sialidases. Chembiochem, 13, 2374-2383. PubMed id: 23070966
Date:
21-Jun-12     Release date:   31-Oct-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q54727  (NANB_STRPN) -  Sialidase B
Seq:
Struc:
 
Seq:
Struc:
697 a.a.
658 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.18  - Exo-alpha-sialidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     exo-alpha-sialidase activity     1 term  

 

 
Chembiochem 13:2374-2383 (2012)
PubMed id: 23070966  
 
 
Synthesis and structural characterisation of selective non-carbohydrate-based inhibitors of bacterial sialidases.
P.Brear, J.Telford, G.L.Taylor, N.J.Westwood.
 
  ABSTRACT  
 
The major human pathogen Streptococcus pneumoniae plays a key role in several disease states including septicaemia, meningitis and community-acquired pneumonia. Although vaccines against S. pneumoniae are available as prophylactics, there remains a need to identify and characterise novel chemical entities that can treat the diseases caused by this pathogen. S. pneumoniae expresses three sialidases, enzymes that cleave sialic acid from carbohydrate-based surface molecules. Two of these enzymes, NanA and NanB, have been implicated in the pathogenesis of S. pneumoniae and are considered to be validated drug targets. Here we report our studies on the synthesis and structural characterisation of novel NanB-selective inhibitors that are inspired by the β-amino-sulfonic acid family of buffers.