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PDBsum entry 3f5k

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3f5k
Jmol
Contents
Protein chains
472 a.a. *
Ligands
CE5 ×2
SO4 ×2
MES ×2
GOL ×2
Metals
_ZN
Waters ×801
* Residue conservation analysis
PDB id:
3f5k
Name: Hydrolase
Title: Semi-active e176q mutant of rice bglu1, a plant exoglucanase glucosidase
Structure: Beta-glucosidase. Chain: a, b. Fragment: unp residues 29-504. Engineered: yes. Mutation: yes
Source: Oryza sativa japonica group. Japanese rice. Organism_taxid: 39947. Strain: orion. Gene: os3bglu7. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.80Å     R-factor:   0.178     R-free:   0.210
Authors: W.Chuenchor,J.R.Ketudat Cairns,S.Pengthaisong,R.C.Robinson, J.Yuvaniyama,C.-J.Chen
Key ref: W.Chuenchor et al. (2011). The structural basis of oligosaccharide binding by rice BGlu1 beta-glucosidase. J Struct Biol, 173, 169-179. PubMed id: 20884352 DOI: 10.1016/j.jsb.2010.09.021
Date:
03-Nov-08     Release date:   03-Nov-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q75I93  (BGL07_ORYSJ) -  Beta-glucosidase 7
Seq:
Struc:
504 a.a.
472 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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!
  Cellular component     extracellular region   1 term 
  Biological process     metabolic process   2 terms 
  Biochemical function     hydrolase activity     16 terms  

 

 
DOI no: 10.1016/j.jsb.2010.09.021 J Struct Biol 173:169-179 (2011)
PubMed id: 20884352  
 
 
The structural basis of oligosaccharide binding by rice BGlu1 beta-glucosidase.
W.Chuenchor, S.Pengthaisong, R.C.Robinson, J.Yuvaniyama, J.Svasti, J.R.Cairns.
 
  ABSTRACT  
 
No abstract given.