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PDBsum entry 2wc3

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protein ligands links
Hydrolase PDB id
2wc3
Jmol
Contents
Protein chains
442 a.a. *
Ligands
AM3 ×4
Waters ×1118
* Residue conservation analysis
PDB id:
2wc3
Name: Hydrolase
Title: Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-oxa-(+)-8-epi- castanospermine
Structure: Beta-glucosidase a. Chain: a, b, c, d. Fragment: residues 2-446. Synonym: beta-glucosidase, gentiobiase, cellobiase, beta-d-glucoside glucohydrolase. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.00Å     R-factor:   0.187     R-free:   0.249
Authors: M.Aguilar,T.M.Gloster,J.P.Turkenburg,M.I.Garcia-Moreno, C.Ortiz Mellet,G.J.Davies,J.M.Garcia Fernandez
Key ref: M.Aguilar-Moncayo et al. (2009). Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring. Org Biomol Chem, 7, 2738-2747. PubMed id: 19532990
Date:
08-Mar-09     Release date:   14-Apr-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q08638  (BGLA_THEMA) -  Beta-glucosidase A
Seq:
Struc:
446 a.a.
442 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.21  - Beta-glucosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   4 terms 
  Biochemical function     hydrolase activity     4 terms  

 

 
Org Biomol Chem 7:2738-2747 (2009)
PubMed id: 19532990  
 
 
Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring.
M.Aguilar-Moncayo, T.M.Gloster, J.P.Turkenburg, M.I.García-Moreno, C.Ortiz Mellet, G.J.Davies, J.M.García Fernández.
 
  ABSTRACT  
 
Synthesis of a panel of iso(thio)urea-type ring-modified castanospermine analogues bearing a freely mutarotating pseudoanomeric hydroxyl group results in tight-binding beta-glucosidase inhibitors with unusual binding signatures; the presence of an N-octyl substituent imparts a remarkable anomeric selectivity, promoting strong binding of the appropriate beta-anomer by the beta-glucosidase.