Sandbox324
From Proteopedia
(Difference between revisions)
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== Proposed Function == | == Proposed Function == | ||
- | This protein has alpha/beta-hydrolase activity and is of the esterase family. The BLAST, InterPro, and Dali Search along with other bioinformatics analyses consistently matched with carboxylesterases and other esterase-like proteins. SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The isolated protein was introduced to 10 mM p-nitrophenyl acetate in a buffer with a pH of 6. Enzyme activity was measured, and the data was consistent with other hydrolases. | + | This protein has alpha/beta-hydrolase activity and is of the esterase family. The SPRITE, BLAST, InterPro, and Dali Search along with other bioinformatics analyses consistently matched with carboxylesterases and other esterase-like proteins. SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The isolated protein was introduced to 10 mM p-nitrophenyl acetate in a buffer with a pH of 6. Enzyme activity was measured, and the data was consistent with other hydrolases. |
[[Image:Enzyme_Activity.jpeg]] | [[Image:Enzyme_Activity.jpeg]] | ||
== Structural highlights == | == Structural highlights == |
Revision as of 19:14, 24 April 2024
Protein 4DIU: Structure, Function, and Significance in Biological Systems
Think of this like an abstract. Include a few sentences about the most important data you found about what type of enzyme this is.
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644