Molecular docking of Sulfobacillus acidophilus barbiturase with s-triazine compounds
- Published
- Accepted
- Subject Areas
- Biochemistry, Bioinformatics, Computational Biology, Environmental Sciences, Microbiology
- Keywords
- barbiturase, molecular docking, s-triazine compounds, homology modeling, in silico
- Copyright
- © 2016 Basharat et al.
- Licence
- This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ Preprints) and either DOI or URL of the article must be cited.
- Cite this article
- 2016. Molecular docking of Sulfobacillus acidophilus barbiturase with s-triazine compounds. PeerJ Preprints 4:e2070v1 https://doi.org/10.7287/peerj.preprints.2070v1
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.
Author Comment
The current pre-print version (v.01) of this manuscript may contain grammatical & proofreading mistakes. Errors and omissions excepted.