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PDBsum entry 3cuj

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protein ligands links
Hydrolase PDB id
3cuj
Jmol
Contents
Protein chain
314 a.a. *
Ligands
X5S
Waters ×366
* Residue conservation analysis
PDB id:
3cuj
Name: Hydrolase
Title: Cellulomonas fimi xylanase/cellulase cex (cf xyn10a) in complex with sulfur substituted beta-1,4 xylopentaose.
Structure: Exo-beta-1,4-glucanase. Chain: a. Fragment: sequence database residues 43-357. Synonym: cellulomonas fimi family 10 xylanase/cellulase. Beta 1,4 endo-xylanase. Cex. Cf xyn10a. Engineered: yes
Source: Cellulomonas fimi. Organism_taxid: 1708. Gene: cex. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.70Å     R-factor:   0.158     R-free:   0.170
Authors: D.A.Kuntz,M.Saul,D.R.Rose
Date:
16-Apr-08     Release date:   21-Apr-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07986  (GUX_CELFI) -  Exoglucanase/xylanase
Seq:
Struc:
484 a.a.
314 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: E.C.3.2.1.8  - Endo-1,4-beta-xylanase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.
   Enzyme class 2: E.C.3.2.1.91  - Cellulose 1,4-beta-cellobiosidase (non-reducing end).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     1 term