PDBsum entry 1pvx

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protein links
Hydrolase PDB id
Protein chain
194 a.a. *
Waters ×128
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Do-1,4-beta-xylanase, room temperature, ph 4.5
Structure: Protein (endo-1,4-beta-xylanase). Chain: a. Synonym: xyla. Ec:
Source: Paecilomyces variotii. Organism_taxid: 45996
1.59Å     R-factor:   0.191     R-free:   0.219
Authors: P.Rajeshkumar,S.Eswaramoorthy,P.J.Vithayathil,M.A.Viswamitra
Key ref: S.Eswaramoorthy et al. (1994). Crystallization and preliminary X-ray crystallographic studies of thermostable xylanase crystals isolated from Paecilomyces varioti. J Mol Biol, 243, 806-808. PubMed id: 7966300
20-Oct-98     Release date:   20-Oct-99    
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Protein chain
Pfam   ArchSchema ?
P81536  (XYNA_PAEVA) -  Endo-1,4-beta-xylanase
194 a.a.
194 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - 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  


J Mol Biol 243:806-808 (1994)
PubMed id: 7966300  
Crystallization and preliminary X-ray crystallographic studies of thermostable xylanase crystals isolated from Paecilomyces varioti.
S.Eswaramoorthy, P.J.Vithayathil, M.A.Viswamitra.
A highly thermostable xylanase isolated from the thermophilic fungus Paecilomyces varioti has been crystallized by the vapour diffusion method. The isolation of this enzyme by crystallization directly from the culture filtrate projects this fungus as an important source for large-scale production of pure xylanase. The crystals belong to orthorhombic space group P2(1)2(1)2(1) with the unit cell dimensions a = 38.48 A, b = 53.87 A and c = 90.23 A. Four molecules occupy a volume of 187,039.4 A3 along with 34% of solvent. The data collected with an area detector to the resolution of 2.7 A were used to calculate the unit cell parameters and Matthews' constant. The optical behaviour of the crystal was studied at different temperatures to understand its thermal stability.

Literature references that cite this PDB file's key reference

  PubMed id Reference
11717493 J.Wouters, J.Georis, D.Engher, J.Vandenhaute, J.Dusart, J.M.Frere, E.Depiereux, and P.Charlier (2001).
Crystallographic analysis of family 11 endo-beta-1,4-xylanase Xyl1 from Streptomyces sp. S38.
  Acta Crystallogr D Biol Crystallogr, 57, 1813-1819.
PDB code: 1hix
10974122 R.Maheshwari, G.Bharadwaj, and M.K.Bhat (2000).
Thermophilic fungi: their physiology and enzymes.
  Microbiol Mol Biol Rev, 64, 461-488.  
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