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 Chinese
| WPRIM
| ID: wpr-327959
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:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Protein Binding
/
Substrate Specificity
/
Bacillus
/
Bacterial Proteins
/
Xylans
/
Computer Simulation
/
Molecular Sequence Data
/
Base Sequence
/
Models, Molecular
/
Amino Acid Sequence
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2007
Type:
Article
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