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PDBsum entry 2vi0

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protein ligands links
Hydrolase PDB id
2vi0
Jmol
Contents
Protein chain
275 a.a. *
Ligands
VAM
BGC-BGC
Waters ×380
* Residue conservation analysis
PDB id:
2vi0
Name: Hydrolase
Title: Lichenase ctlic26 in complex with a thio-oligosaccharide
Structure: Endoglucanase h. Chain: a. Fragment: residues 26-304. Synonym: ctlic26a, egh, cellulase h, endo-1,4-beta-glucanase h. Mutation: yes
Source: Clostridium thermocellum. Organism_taxid: 1515. Atcc: 13950
Resolution:
1.51Å     R-factor:   0.154     R-free:   0.189
Authors: V.A.Money,V.M.Ducros,G.J.Davies
Key ref: V.A.Money et al. (2008). Probing the beta-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants. Org Biomol Chem, 6, 851-853. PubMed id: 18292875
Date:
26-Nov-07     Release date:   10-Mar-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P16218  (GUNH_CLOTH) -  Endoglucanase H
Seq:
Struc:
 
Seq:
Struc:
900 a.a.
275 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.4  - Cellulase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   2 terms 
  Biochemical function     cellulase activity     2 terms  

 

 
Org Biomol Chem 6:851-853 (2008)
PubMed id: 18292875  
 
 
Probing the beta-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants.
V.A.Money, A.Cartmell, C.I.Guerreiro, V.M.Ducros, C.M.Fontes, H.J.Gilbert, G.J.Davies.
 
  ABSTRACT  
 
The substrate binding regions of a beta-1,3:1,4 glucanase are revealed through structural analysis with a thio-oligosaccharide and kinetics of enzyme variants.