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PDBsum entry 4dgr

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protein ligands metals links
Hydrolase/hydrolase inhibitor PDB id
4dgr
Jmol
Contents
Protein chain
389 a.a.
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN-MAN-MAN-
MAN
NAG-NAG
NAG-NAG-BMA
BGC ×3
GLC
3LV
PO4
Metals
__K
_CA ×2
Waters ×483
PDB id:
4dgr
Name: Hydrolase/hydrolase inhibitor
Title: Influenza subtype 9 neuraminidase benzoic acid inhibitor com
Structure: Neuraminidase. Chain: a. Fragment: neuraminidase. Ec: 3.2.1.18
Source: Influenza a virus (a/tern/australia/g70c/1975(h11n9)). Organism_taxid: 384509. Strain: h1n9 avian influenza
Resolution:
1.55Å     R-factor:   0.123     R-free:   0.152
Authors: L.Venkatramani,E.Johnson,G.Kolavi,G.M.Air,W.Brouillette,B.H.
Key ref: L.Venkatramani et al. (2012). Crystal structure of a new benzoic acid inhibitor of influenza neuraminidase bound with a new tilt induced by overpacking subsite C6. BMC Struct Biol, 12, 7. PubMed id: 22559154 DOI: 10.1186/1472-6807-12-7
Date:
26-Jan-12     Release date:   16-May-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P03472  (NRAM_I75A5) -  Neuraminidase
Seq:
Struc:
470 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  

 

 
DOI no: 10.1186/1472-6807-12-7 BMC Struct Biol 12:7 (2012)
PubMed id: 22559154  
 
 
Crystal structure of a new benzoic acid inhibitor of influenza neuraminidase bound with a new tilt induced by overpacking subsite C6.
L.Venkatramani, E.S.Johnson, G.Kolavi, G.M.Air, W.J.Brouillette, B.H.Mooers.
 
  ABSTRACT  
 
No abstract given.