Conclusion

Chapter
Part of the SpringerBriefs in Systems Biology book series (BRIEFSBIOSYS)

Abstract

The identification of a high-quality binding site and depiction of a target protein is of prime significance that leads to its functional annotations. In the present work, diverse binding site residues viz. Trp18, Asn44, Val46, Tyr73, Tyr77, Ala176, Glu178 were studied using SYBYL and it was envisaged that Tyr77 was conserved in family 11 xylanases. Furthermore, during residue conservation analysis through ConSurf method Tyr77 was observed as highly conserved among others. Molecular docking of endo-1, 4-beta xylanases (1YNA) with substrates viz. xylobiose and beta-D-xylopyranose established Tyr77 residue as conserved in both the binding sites and InterProScan analysis further verified Tyr77 in family 11 glycoside hydrolase motifs with a significantly good score of 1,604.

Keywords

Val46 Glycoside Hydrolase Xylobiose 

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Copyright information

© The Author(s) 2012

Authors and Affiliations

  1. 1.Department of BiotechnologyBirla Institute of Technology (Deemed University)MesraIndia
  2. 2.Enzyme Technology and Protein Bioinformatics Laboratory, Department of MicrobiologyMaharshi Dayanand UniversityHaryanaIndia

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