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PDBsum entry 3k36

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3k36
Jmol
Contents
Protein chains
389 a.a.
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN
×2
SO4 ×2
EDO ×2
GOL ×4
Metals
_CA ×2
Waters ×316
PDB id:
3k36
Name: Hydrolase
Title: Crystal structure of b/perth neuraminidase
Structure: Neuraminidase. Chain: a, b. Fragment: unp residues 70-466. Engineered: yes
Source: Influenza b virus. Viruses. Organism_taxid: 343983. Strain: b/perth/211/2001. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf21.
Resolution:
2.20Å     R-factor:   0.185     R-free:   0.239
Authors: A.J.Oakley,J.L.Mckimm-Breschkin
Key ref: A.J.Oakley et al. (2010). Structural and functional basis of resistance to neuraminidase inhibitors of influenza B viruses. J Med Chem, 53, 6421-6431. PubMed id: 20695427
Date:
02-Oct-09     Release date:   01-Sep-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q3S340  (Q3S340_9INFB) -  Neuraminidase
Seq:
Struc:
466 a.a.
389 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!
  Cellular component     membrane   3 terms 
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     exo-alpha-sialidase activity     1 term  

 

 
J Med Chem 53:6421-6431 (2010)
PubMed id: 20695427  
 
 
Structural and functional basis of resistance to neuraminidase inhibitors of influenza B viruses.
A.J.Oakley, S.Barrett, T.S.Peat, J.Newman, V.A.Streltsov, L.Waddington, T.Saito, M.Tashiro, J.L.McKimm-Breschkin.
 
  ABSTRACT  
 
No abstract given.