Sandbox Reserved 1674

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== Structural highlights ==
== Structural highlights ==
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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>.
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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 thos<scene name='87/873236/Chain_a_active_site/1'>e catalytic amino acids</scene>, which have been highlighted <scene name='87/873236/Active_site_red/1'>here</scene>.
== Other important features ==
== Other important features ==

Revision as of 15:54, 16 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.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

CTX-M Beta-Lactamase

Overall structure of CTX-M Beta-Lactamase without any important ligands. (PDB: 7K2X)

Drag the structure with the mouse to rotate

References

[1]

  1. ↑ 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
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