PDBsum entry 2jal

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
436 a.a. *
YLL ×2
ACT ×2
Waters ×474
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Beta-glucosidase from thermotoga maritima in complex with cyclophellitol
Structure: Beta-glucosidase a. Chain: a, b. 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: 511693.
1.90Å     R-factor:   0.198     R-free:   0.244
Authors: T.M.Gloster,R.Madsen,G.J.Davies
Key ref: T.M.Gloster et al. (2007). Structural basis for cyclophellitol inhibition of a beta-glucosidase. Org Biomol Chem, 5, 444-446. PubMed id: 17252125
29-Nov-06     Release date:   03-Jan-07    
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Protein chains
Pfam   ArchSchema ?
Q08638  (BGLA_THEMA) -  Beta-glucosidase A
446 a.a.
436 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - 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 5:444-446 (2007)
PubMed id: 17252125  
Structural basis for cyclophellitol inhibition of a beta-glucosidase.
T.M.Gloster, R.Madsen, G.J.Davies.
The structural basis for beta-glucosidase inhibition by cyclophellitol is demonstrated using X-ray crystallography, enzyme kinetics and mass spectrometry.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21079602 M.D.Witte, W.W.Kallemeijn, J.Aten, K.Y.Li, A.Strijland, W.E.Donker-Koopman, A.M.van den Nieuwendijk, B.Bleijlevens, G.Kramer, B.I.Florea, B.Hooibrink, C.E.Hollak, R.Ottenhoff, R.G.Boot, G.A.van der Marel, H.S.Overkleeft, and J.M.Aerts (2010).
Ultrasensitive in situ visualization of active glucocerebrosidase molecules.
  Nat Chem Biol, 6, 907-913.  
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