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PDBsum entry 2l8a

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protein links
Hydrolase PDB id
2l8a
Jmol
Contents
Protein chain
149 a.a.
PDB id:
2l8a
Name: Hydrolase
Title: Structure of a novel cbm3 lacking the calcium-binding site
Structure: Endoglucanase. Chain: a. Fragment: cbm3 domain residues 354-499. Synonym: carboxymethyl-cellulase, cmcase, cellulase, endo-1 glucanase. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Gene: egls, bglc, gld, bsu18130. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: J.H.Paiva,A.N.Meza,M.L.Sforca,R.Z.Navarro,J.L.Neves,C.R.Sant M.T.Murakami,A.C.Zeri
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:
07-Jan-11     Release date:   21-Dec-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P10475  (GUN2_BACSU) -  Endoglucanase
Seq:
Struc:
499 a.a.
149 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 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     carbohydrate binding     2 terms  

 

 
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.