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PDBsum entry 4cpy

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4cpy

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
390 a.a.
Ligands
NAG-NAG ×2
NAG ×2
G39 ×2
EDO ×17
Metals
_CA ×2
Waters ×703
PDB id:
4cpy
Name: Hydrolase
Title: Structure of the neuraminidase from the b/lyon/chu/15.216/2011 virus in complex with oseltamivir
Structure: Neuraminidase. Chain: a, b. Ec: 3.2.1.18
Source: Influenza b virus. Organism_taxid: 11520. Strain: b/lyon/chu/15.216/2011
Resolution:
1.80Å     R-factor:   0.172     R-free:   0.179
Authors: S.G.Vachieri,P.J.Collins,V.Escuret,J.S.Casalegno,N.Cattle,O.Ferraris, M.Sabatier,E.Frobert,V.Caro,J.J.Skehel,S.J.Gamblin,F.Valla, M.Valette,M.Ottmann,J.W.Mccauley,R.S.Daniels,B.Lina
Key ref: V.Escuret et al. (2014). A novel I221L substitution in neuraminidase confers high-level resistance to oseltamivir in influenza B viruses. J Infect Dis, 210, 1260-1269. PubMed id: 24795482 DOI: 10.1093/infdis/jiu244
Date:
09-Feb-14     Release date:   14-May-14    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
U5XBU0  (U5XBU0_9INFB) -  Neuraminidase from Influenza B virus
Seq:
Struc:
466 a.a.
390 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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.

 

 
DOI no: 10.1093/infdis/jiu244 J Infect Dis 210:1260-1269 (2014)
PubMed id: 24795482  
 
 
A novel I221L substitution in neuraminidase confers high-level resistance to oseltamivir in influenza B viruses.
V.Escuret, P.J.Collins, J.S.Casalegno, S.G.Vachieri, N.Cattle, O.Ferraris, M.Sabatier, E.Frobert, V.Caro, J.J.Skehel, S.Gamblin, F.Valla, M.Valette, M.Ottmann, J.W.McCauley, R.S.Daniels, B.Lina.
 
  ABSTRACT  
 
No abstract given.

 

 

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