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PDBsum entry 3mfc

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protein ligands links
Hydrolase PDB id
3mfc
Jmol
Contents
Protein chain
187 a.a. *
Ligands
SO4 ×2
Waters ×219
* Residue conservation analysis
PDB id:
3mfc
Name: Hydrolase
Title: Computationally designed end0-1,4-beta,xylanase
Structure: Endo-1,4-beta-xylanase. Chain: a. Fragment: unp residues 44-235. Engineered: yes. Mutation: yes
Source: Thermopolyspora flexuosa. Organism_taxid: 103836. Gene: xyn11a. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.70Å     R-factor:   0.140     R-free:   0.189
Authors: A.Morin,J.M.Harp
Key ref: A.Morin et al. (2011). Computational design of an endo-1,4-beta-xylanase ligand binding site. Protein Eng Des Sel, 24, 503-516. PubMed id: 21349882
Date:
01-Apr-10     Release date:   10-Nov-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8GMV7  (Q8GMV7_9ACTO) -  Endo-1,4-beta-xylanase
Seq:
Struc:
344 a.a.
187 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: 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.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     1 term  

 

 
Protein Eng Des Sel 24:503-516 (2011)
PubMed id: 21349882  
 
 
Computational design of an endo-1,4-beta-xylanase ligand binding site.
A.Morin, K.W.Kaufmann, C.Fortenberry, J.M.Harp, L.S.Mizoue, J.Meiler.
 
  ABSTRACT  
 
No abstract given.