spacer
spacer

PDBsum entry 2v3g

Go to PDB code: 
protein ligands links
Hydrolase PDB id
2v3g
Jmol
Contents
Protein chain
273 a.a. *
Ligands
BGC-NOY
Waters ×488
* Residue conservation analysis
PDB id:
2v3g
Name: Hydrolase
Title: Structure of a family 26 lichenase in complex with noeuromycin
Structure: Endoglucanase h. Chain: a. Fragment: catalytic domain, residues 26-305. Synonym: egh, endo-1,4-beta-glucanase h, cellulase h, lichenase. Engineered: yes
Source: Clostridium thermocellum. Organism_taxid: 1515. Strain: f1/ys. Atcc: 27405. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.20Å     R-factor:   0.117     R-free:   0.144
Authors: P.J.Meloncelli,T.M.Gloster,V.A.Money,C.A.Tarling,G.J.Davies, S.G.Withers,R.V.Stick
Key ref: P.J.Meloncelli et al. D-Glucosylated derivatives of isofagomine and noeuromycin and their potential as inhibitors of beta-Glycoside hydrolases. To be published, .
Date:
18-Jun-07     Release date:   18-Sep-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P16218  (GUNH_CLOTH) -  Endoglucanase H
Seq:
Struc:
 
Seq:
Struc:
900 a.a.
273 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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