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PDBsum entry 2xzk

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2xzk
Jmol
Contents
Protein chains
385 a.a. *
Ligands
FKD ×2
K99 ×5
GOL ×5
NO3
Metals
_CL ×2
_NA ×2
Waters ×1095
* Residue conservation analysis
PDB id:
2xzk
Name: Hydrolase
Title: The aspergillus fumigatus sialidase is a kdnase: structural and mechanistic insights
Structure: Extracellular sialidase/neuraminidase, putative. Chain: a, b. Fragment: mature protein, residues 21-406. Synonym: kdnase. Engineered: yes
Source: Aspergillus fumigatus. Organism_taxid: 330879. Strain: af293. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.50Å     R-factor:   0.180     R-free:   0.213
Authors: J.C.Telford,J.H.F.Yeung,M.J.Kiefel,A.G.Watts,S.Hader,J.Chan, A.J.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 DOI: 10.1074/jbc.M110.207043
Date:
26-Nov-10     Release date:   19-Jan-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q4WQS0  (Q4WQS0_ASPFU) -  Exo-alpha-sialidase
Seq:
Struc:
406 a.a.
385 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   4 terms 
  Biochemical function     exo-alpha-(2->3)-sialidase activity     6 terms  

 

 
DOI no: 10.1074/jbc.M110.207043 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.