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PDBsum entry 2xcy

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2xcy
Jmol
Contents
Protein chains
386 a.a. *
Ligands
GOL
Metals
_CL ×2
Waters ×1049
* Residue conservation analysis
PDB id:
2xcy
Name: Hydrolase
Title: Crystal structure of aspergillus fumigatus sialidase
Structure: Extracellular sialidase/neuraminidase, putative. Chain: a, b. Fragment: residues 21-406. Engineered: yes
Source: Aspergillus fumigatus. Organism_taxid: 5085. Atcc: atcc 13073. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.84Å     R-factor:   0.155     R-free:   0.194
Authors: J.C.Telford,J.Yeung,G.Xu,A.Bennet,M.M.Moore,G.L.Taylor
Key ref: J.C.Telford et al. (2011). The Aspergillus fumigatus sialidase is a 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid hydrolase (KDNase): structural and mechanistic insights. J Biol Chem, 286, 10783-10792. PubMed id: 21247893
Date:
27-Apr-10     Release date:   12-May-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q4WQS0  (Q4WQS0_ASPFU) -  Extracellular sialidase/neuraminidase, putative
Seq:
Struc:
406 a.a.
386 a.a.
Key:    PfamA domain  PfamB 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     cellular_component   1 term 
  Biological process     biological_process   2 terms 
  Biochemical function     exo-alpha-(2->3)-sialidase activity     7 terms  

 

 
J Biol Chem 286:10783-10792 (2011)
PubMed id: 21247893  
 
 
The Aspergillus fumigatus sialidase is a 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid hydrolase (KDNase): structural and mechanistic insights.
J.C.Telford, J.H.Yeung, G.Xu, M.J.Kiefel, A.G.Watts, S.Hader, J.Chan, A.J.Bennet, M.M.Moore, G.L.Taylor.
 
  ABSTRACT  
 
No abstract given.