Sandbox Reserved 1674
From Proteopedia
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CTX-M Beta-Lactamase is an enzyme made to inhibit Beta-Lactam. It is found within the E.Coli bacteria and makes the bacteria drug resistant. | CTX-M Beta-Lactamase is an enzyme made to inhibit Beta-Lactam. It is found within the E.Coli bacteria and makes the bacteria drug resistant. | ||
- | == | + | == Function of your protein == |
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- | == | + | == Biological relevance and broader implications == |
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+ | == Important amino acids== | ||
== Structural highlights == | == Structural highlights == | ||
+ | This protein has eight chains. <scene name='87/873236/Chain_a/1'>Each chain</scene> has eleven separate alpha helixes, and nine separate beta sheets. Some of the chains do bind to a GOL to help with stability. Within each chain, there are two of the catalytic amino acids within helix three. The last catalytic amino acid is located in helix seven. Both of those helices form important interactions with the ligands because of those catalytic amino acids, which have been highlighted <scene name='87/873236/Active_site_red/1'>here</scene>. | ||
+ | == Other important features == | ||
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. |
Revision as of 13:57, 7 April 2021
This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682. |
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CTX-M Beta-Lactamase
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References
- ↑ Soeung V, Lu S, Hu L, Judge A, Sankaran B, Prasad BVV, Palzkill T. A drug-resistant beta-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency. J Biol Chem. 2020 Dec 25;295(52):18239-18255. doi: 10.1074/jbc.RA120.016103. Epub, 2020 Oct 26. PMID:33109613 doi:http://dx.doi.org/10.1074/jbc.RA120.016103