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PDBsum entry 2cks

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2cks
Jmol
Contents
Protein chains
305 a.a. *
Ligands
BEN ×2
Metals
_NA ×4
_ZN ×8
Waters ×640
* Residue conservation analysis
PDB id:
2cks
Name: Hydrolase
Title: X-ray crystal structure of the catalytic domain of thermobifida fusca endoglucanase cel5a (e5)
Structure: Endoglucanase e-5. Chain: a, b. Fragment: catalytic domain, residues 161-466. Synonym: endoglucanase cel5a, endo-1,4-beta-glucanase e-4, cellulase e-5, cellulase e5. Engineered: yes
Source: Thermobifida fusca. Organism_taxid: 2021. Expressed in: bacillus subtilis. Expression_system_taxid: 1423.
Resolution:
1.60Å     R-factor:   0.142     R-free:   0.169
Authors: G.I.Berglund,P.J.Gualfetti,C.Requadt,L.S.Gross,T.Bergfors, A.Shaw,M.Saldajeno,C.Mitchinson,M.Sandgren
Key ref: G.I.Berglund et al. The crystal structure of the catalytic domain of thermobifida fusca endoglucanase cel5a in complex with cellotetraose. To be published, .
Date:
21-Apr-06     Release date:   29-May-07    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q01786  (GUN5_THEFU) -  Endoglucanase E-5
Seq:
Struc:
466 a.a.
305 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   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     1 term