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PDBsum entry 3o2l

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protein links
Hydrolase PDB id
3o2l
Jmol
Contents
Protein chain
306 a.a.
Waters ×204
PDB id:
3o2l
Name: Hydrolase
Title: Crystal structure of an inactive kemp elimination design hg-
Structure: Endo-1,4-beta-xylanase. Chain: a. Fragment: unp residues 27-329. Synonym: xylanase, 1,4-beta-d-xylan xylanohydrolase, taxi. Engineered: yes. Mutation: yes
Source: Thermoascus aurantiacus. Organism_taxid: 5087. Gene: xyna. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.170     R-free:   0.229
Authors: L.M.Thomas,H.K.Privett,S.L.Mayo
Key ref: H.K.Privett et al. (2012). Iterative approach to computational enzyme design. Proc Natl Acad Sci U S A, 109, 3790-3795. PubMed id: 22357762 DOI: 10.1073/pnas.1118082108
Date:
22-Jul-10     Release date:   20-Jul-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P23360  (XYNA_THEAU) -  Endo-1,4-beta-xylanase
Seq:
Struc:
329 a.a.
306 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 9 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     metabolic process   4 terms 
  Biochemical function     hydrolase activity     4 terms  

 

 
DOI no: 10.1073/pnas.1118082108 Proc Natl Acad Sci U S A 109:3790-3795 (2012)
PubMed id: 22357762  
 
 
Iterative approach to computational enzyme design.
H.K.Privett, G.Kiss, T.M.Lee, R.Blomberg, R.A.Chica, L.M.Thomas, D.Hilvert, K.N.Houk, S.L.Mayo.
 
  ABSTRACT  
 
No abstract given.