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PDBsum entry 3ac0

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3ac0

 

 

 

 

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Contents
Protein chains
841 a.a. *
Ligands
BGC ×4
Waters ×1564
* Residue conservation analysis
PDB id:
3ac0
Name: Hydrolase
Title: Crystal structure of beta-glucosidase from kluyveromyces marxianus in complex with glucose
Structure: Beta-glucosidase i. Chain: a, b, c, d. Engineered: yes
Source: Kluyveromyces marxianus. Yeast. Organism_taxid: 4911. Strain: nbrc1777. Gene: bgl, bgli. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.54Å     R-factor:   0.173     R-free:   0.242
Authors: E.Yoshida,M.Hidaka,S.Fushinobu,T.Katayama,H.Kumagai
Key ref: E.Yoshida et al. (2010). Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 β-glucosidase from Kluyveromyces marxianus. Biochem J, 431, 39-49. PubMed id: 20662765
Date:
25-Dec-09     Release date:   11-Aug-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
D1GCC6  (D1GCC6_KLUMA) -  beta-glucosidase from Kluyveromyces marxianus
Seq:
Struc:
 
Seq:
Struc:
845 a.a.
841 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.

 

 
Biochem J 431:39-49 (2010)
PubMed id: 20662765  
 
 
Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 β-glucosidase from Kluyveromyces marxianus.
E.Yoshida, M.Hidaka, S.Fushinobu, T.Koyanagi, H.Minami, H.Tamaki, M.Kitaoka, T.Katayama, H.Kumagai.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21219452 D.Dodd, R.I.Mackie, and I.K.Cann (2011).
Xylan degradation, a metabolic property shared by rumen and human colonic Bacteroidetes.
  Mol Microbiol, 79, 292-304.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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