Molecular docking of Bacillus pumilus xylanase and xylan substrate using computer modeling / 生物工程学报
Chinese Journal of Biotechnology
; (12): 715-718, 2007.
Article
in Zh
| WPRIM
| ID: wpr-327959
Responsible library:
WPRO
ABSTRACT
Bacillus pumilus xylanase was cloned and sequenced. Based on the tertiary structure that originated from homology modeling, the potential active pocket was searched and ligand-protein docking was performed using relative softwares. The information extracted from the molecular docking is analyzed; several amino acid residues might play a vital role in the xylanase catalytic reaction are obtained to instruct the further modification of xylanase directed-evolution.
Full text:
1
Index:
WPRIM
Main subject:
Protein Binding
/
Substrate Specificity
/
Bacillus
/
Bacterial Proteins
/
Xylans
/
Computer Simulation
/
Molecular Sequence Data
/
Base Sequence
/
Models, Molecular
/
Amino Acid Sequence
Language:
Zh
Journal:
Chinese Journal of Biotechnology
Year:
2007
Type:
Article