Sandbox Reserved 1697
From Proteopedia
(Difference between revisions)
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== Important amino acids== | == Important amino acids== | ||
- | In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. | + | In the protein seen in the paper there is a mutation at residue 54, causing an <scene name='89/892740/Mutation_scence/1'>aspartic acid to change to an alanine</scene>. The catalytic amino acids are Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313. |
== Structural highlights == | == Structural highlights == | ||
+ | This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is 77% helix and 23% beta sheet, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. | ||
== Other important features == | == Other important features == |
Revision as of 00:51, 8 November 2021
This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699. |
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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