Molecular docking of Sulfobacillus acidophilus barbiturase with s-triazine compounds
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Abstract
Barbiturases have scarce structural information available and do not fit in the conventional group of proteins. It is contemplated that they play a role in catabolism of s-triazine herbicide compounds. Structure as well as interaction data information of barbiturase with s-triazine compounds is missing. Sequence data is a goldmine of biological information and acts as raw material for structure and docking analysis. De novo structure prediction of the Sulfobacillus acidophilus DSM 10332 barbiturase has been attempted in this data article. Molecular docking analysis was carried out with atrazine, simazine and hexazinone belonging to s-triazine class of herbicides. The analysis revealed key residues necessary for these interactions. The generated data could be used by environmental scientists working on the enzyme assisted herbicide degradation.
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2016. Molecular docking of Sulfobacillus acidophilus barbiturase with s-triazine compounds. PeerJ Preprints 4:e2070v1 https://doi.org/10.7287/peerj.preprints.2070v1Author comment
The current pre-print version (v.01) of this manuscript may contain grammatical & proofreading mistakes. Errors and omissions excepted.
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Competing Interests
The authors declare that they have no competing interests.
Author Contributions
Zarrin Basharat conceived and designed the experiments, performed the experiments, analyzed the data, wrote the paper, prepared figures and/or tables.
Azra Yasmin contributed reagents/materials/analysis tools, reviewed drafts of the paper.
Data Deposition
The following information was supplied regarding data availability:
The raw data has been supplied as a supplemental dataset.
Funding
The authors received no funding for this work.
