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PDBsum entry 3vhn

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3vhn
Jmol
Contents
Protein chains
(+ 2 more) 255 a.a.
Ligands
CBI ×8
Waters ×849
PDB id:
3vhn
Name: Hydrolase
Title: Y61g mutant of cellulase 12a from thermotoga maritima
Structure: Endo-1,4-beta-glucanase. Chain: a, b, c, d, e, f, g, h. Synonym: cellulase 12a. Engineered: yes. Mutation: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: cela. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.185     R-free:   0.245
Authors: Y.-S.Cheng,T.-P.Ko,R.-T.Guo,J.-R.Liu
Key ref: Y.S.Cheng et al. (2012). Enhanced activity of Thermotoga maritima cellulase 12A by mutating a unique surface loop. Appl Microbiol Biotechnol, 95, 661-669. PubMed id: 22170108 DOI: 10.1007/s00253-011-3791-4
Date:
30-Aug-11     Release date:   11-Jul-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q60032  (Q60032_THEMT) -  Endo-1,4-beta-glucanase
Seq:
Struc:
257 a.a.
255 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     metabolic process   3 terms 
  Biochemical function     hydrolase activity     4 terms  

 

 
DOI no: 10.1007/s00253-011-3791-4 Appl Microbiol Biotechnol 95:661-669 (2012)
PubMed id: 22170108  
 
 
Enhanced activity of Thermotoga maritima cellulase 12A by mutating a unique surface loop.
Y.S.Cheng, T.P.Ko, J.W.Huang, T.H.Wu, C.Y.Lin, W.Luo, Q.Li, Y.Ma, C.H.Huang, A.H.Wang, J.R.Liu, R.T.Guo.
 
  ABSTRACT  
 
No abstract given.