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PDBsum entry 4u3a

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protein Protein-protein interface(s) links
Hydrolase PDB id
4u3a

 

 

 

 

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Contents
Protein chains
292 a.a.
Waters ×46
PDB id:
4u3a
Name: Hydrolase
Title: Crystal structure of ctcel5e
Structure: Endoglucanase h. Chain: a, b. Fragment: unp residues 290-654. Synonym: cellulase h,endo-1,4-beta-glucanase h,egh, hcel5e. Engineered: yes
Source: Clostridium thermocellum atcc 27405. Organism_taxid: 203119. Gene: celh, cthe_1472. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.42Å     R-factor:   0.204     R-free:   0.248
Authors: S.F.Yuan,P.H.Liang,M.C.Ho
Key ref: S.F.Yuan et al. (2015). Biochemical characterization and structural analysis of a bifunctional cellulase/xylanase from Clostridium thermocellum. J Biol Chem, 290, 5739-5748. PubMed id: 25575592 DOI: 10.1074/jbc.M114.604454
Date:
19-Jul-14     Release date:   14-Jan-15    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P16218  (GUNH_CLOTH) -  Endoglucanase H from Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Seq:
Struc:
 
Seq:
Struc:
900 a.a.
292 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.

 

 
DOI no: 10.1074/jbc.M114.604454 J Biol Chem 290:5739-5748 (2015)
PubMed id: 25575592  
 
 
Biochemical characterization and structural analysis of a bifunctional cellulase/xylanase from Clostridium thermocellum.
S.F.Yuan, T.H.Wu, H.L.Lee, H.Y.Hsieh, W.L.Lin, B.Yang, C.K.Chang, Q.Li, J.Gao, C.H.Huang, M.C.Ho, R.T.Guo, P.H.Liang.
 
  ABSTRACT  
 
No abstract given.

 

 

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