spacer
spacer

PDBsum entry 2f29

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2f29
Jmol
Contents
Protein chain
370 a.a. *
Ligands
DAN ×2
EPE ×4
Waters ×75
* Residue conservation analysis
PDB id:
2f29
Name: Hydrolase
Title: Crystal structure of the human sialidase neu2 q116e mutant in complex with dana inhibitor
Structure: Sialidase 2. Chain: a, b. Synonym: neu2, cytosolic sialidase, n-acetyl-alpha- neuraminidase 2. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
2.92Å     R-factor:   0.188     R-free:   0.265
Authors: L.M.G.Chavas,R.Kato,P.Fusi,C.Tringali,B.Venerando, G.Tettamanti,E.Monti,S.Wakatsuki
Key ref: L.M.G.Chavas et al. Crystal structure of the human sialidase neu2 q116e mutant in complex with dana inhibitor. To be published, .
Date:
15-Nov-05     Release date:   21-Nov-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9Y3R4  (NEUR2_HUMAN) -  Sialidase-2
Seq:
Struc:
380 a.a.
370 a.a.*
Key:    PfamA domain  PfamB 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.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     metabolic process   9 terms 
  Biochemical function     exo-alpha-(2->3)-sialidase activity     6 terms