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PDBsum entry 3pzu

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3pzu
Jmol
Contents
Protein chains
297 a.a.
Ligands
GOL ×3
Waters ×330
PDB id:
3pzu
Name: Hydrolase
Title: P212121 crystal form of the endo-1,4-beta-glucanase from bac subtilis 168
Structure: Endoglucanase. Chain: a, b. Fragment: catalytic domain, unp residues 27-332. Synonym: carboxymethyl-cellulase, cmcase, cellulase, endo-1 glucanase. Engineered: yes
Source: Bacillus subtilis subsp. Subtilis. Organism_taxid: 224308. Strain: 168. Gene: egls, bglc, gld, bsu18130. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.10Å     R-factor:   0.173     R-free:   0.221
Authors: C.R.Santos,J.H.Paiva,P.K.Akao,A.N.Meza,J.C.Silva,F.M.Squina, R.Ruller,M.T.Murakami
Key ref: C.R.Santos et al. (2012). Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168. Biochem J, 441, 95. PubMed id: 21880019 DOI: 10.1042/BJ20110869
Date:
14-Dec-10     Release date:   14-Sep-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P10475  (GUN2_BACSU) -  Endoglucanase
Seq:
Struc:
499 a.a.
297 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  

 

 
DOI no: 10.1042/BJ20110869 Biochem J 441:95 (2012)
PubMed id: 21880019  
 
 
Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168.
C.R.Santos, J.H.Paiva, M.L.Sforça, J.L.Neves, R.Z.Navarro, J.Cota, P.K.Akao, Z.B.Hoffmam, A.N.Meza, J.H.Smetana, M.L.Nogueira, I.Polikarpov, J.Xavier-Neto, F.M.Squina, R.J.Ward, R.Ruller, A.C.Zeri, M.T.Murakami.
 
  ABSTRACT  
 
No abstract given.