Sandbox2QRU
From Proteopedia
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This is a default text for your page '''Sandbox2QRU'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Sandbox2QRU'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.2210/pdb2QRU/pdb</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.2210/pdb2QRU/pdb</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
+ | The work below details the computational characterization and functional analysis of a protein, 2QRU, with a known crystal structure. Using a variety of computational methods, a variety of key identifiers in the sequences and structure could be isolated to better understand the function of the protein. This is due to the ideology that sequence denotes structure which denotes function. | ||
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+ | 2QRU is known to be a hydrolase, most active on esterase. The structure is 276 amino acids long, which is approximately 30.14 kDa. Knowing 2QRU is an alpha/beta hydrolase, the literature helped give further information on possible experimental conditions and substrates that can be used to identify activity. However, experimental data has not been obtained yet. | ||
- | '''General Structure and Origins''' | ||
- | 2QRU is 31.26 kD over 274 residues. This protein is found in the bacteria Enterococcus faecalis and is known to be a member of the alpha/beta hydrolase family. | ||
- | '''Family and Superfamily''' | ||
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== Structure/Sequence Analysis == | == Structure/Sequence Analysis == | ||
Revision as of 00:38, 28 April 2025
Overview
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References
- ↑ doi: https://dx.doi.org/10.2210/pdb2QRU/pdb
- ↑ 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