spacer
spacer

PDBsum entry 2lro

Go to PDB code: 
protein metals links
Hydrolase PDB id
2lro
Jmol
Contents
Protein chain
172 a.a.
Metals
_CA ×2
PDB id:
2lro
Name: Hydrolase
Title: Solution structure, dynamics and binding studies of ctcbm11
Structure: Endoglucanase h. Chain: a. Fragment: cbm11 domain residues 655-821. Synonym: cellulase h, endo-1,4-beta-glucanase h, egh. Engineered: yes
Source: Clostridium thermocellum. Organism_taxid: 203119. Strain: atcc 27405 / dsm 1237. Gene: celh, cthe_1472. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: A.Viegas,E.J.Cabrita
Key ref: A.Viegas et al. (2013). Solution structure, dynamics and binding studies of a family 11 carbohydrate-binding module from Clostridium thermocellum (CtCBM11). Biochem J, 451, 289-300. PubMed id: 23356867 DOI: 10.1042/BJ20120627
Date:
11-Apr-12     Release date:   06-Feb-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P16218  (GUNH_CLOTH) -  Endoglucanase H
Seq:
Struc:
 
Seq:
Struc:
900 a.a.
172 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 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     cellulose catabolic process   1 term 
  Biochemical function     cellulase activity     1 term  

 

 
DOI no: 10.1042/BJ20120627 Biochem J 451:289-300 (2013)
PubMed id: 23356867  
 
 
Solution structure, dynamics and binding studies of a family 11 carbohydrate-binding module from Clostridium thermocellum (CtCBM11).
A.Viegas, J.Sardinha, F.Freire, D.F.Duarte, A.L.Carvalho, C.M.Fontes, M.J.Romão, A.L.Macedo, E.J.Cabrita.
 
  ABSTRACT  
 
No abstract given.