Sandbox Reserved 1590

From Proteopedia

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<scene name='82/824635/Alpha_helices_of_2cab/1'>helices</scene>
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<scene name='82/824635/Beta_sheets/1'>beta sheets</scene><scene name='82/824635/Alpha_helices_of_2cab/1'>helices</scene>
Anything in this section will appear adjacent to the 3D structure and will be scrollable.
Anything in this section will appear adjacent to the 3D structure and will be scrollable.
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== Structure and Highlights==
== Structure and Highlights==
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The molecular weight of this structure is 28.85kDa with an atom count of 2,010. There are a total of 260 amino acids in this protein, with the first amino acid in the sequence being alanine and the last being phenylalanine. The first four amino acids are not represented in this model. In the center of this protein is a Zn^2+ ion. This structure contains five <scene name='82/824635/Alpha_helices_of_2cab/1'>helices</scene> with a total of 48 amino acids used to form them. They have lengths of approximately 10,8,14,5 and 11 amino acids in respect to chain-sequential order. There are also ten beta sheets formed with a total of 72 amino acids. They have lengths of 3,8,7,10,9,12,6,6,7 and 4 amino acids in respect to chain-sequential order. The beta sheets of this protein form a majority of the inner bulk. They are aligned in a formation in which they all sit upon a common axis. lastly, The beta sheets twist around the Zn^2+ ion to avoid direct contact.
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The molecular weight of this structure is 28.85kDa with an atom count of 2,010. There are a total of 260 amino acids in this protein, with the first amino acid in the sequence being alanine and the last being phenylalanine. The first four amino acids are not represented in this model. In the center of this protein is a Zn^2+ ion. This structure contains five <scene name='82/824635/Alpha_helices_of_2cab/1'>helices</scene> with a total of 48 amino acids used to form them. They have lengths of approximately 10,8,14,5 and 11 amino acids in respect to chain-sequential order. There are also ten <scene name='82/824635/Beta_sheets/1'>beta sheets</scene> formed with a total of 72 amino acids. They have lengths of 3,8,7,10,9,12,6,6,7 and 4 amino acids in respect to chain-sequential order. The beta sheets of this protein form a majority of the inner bulk. They are aligned in a formation in which they all sit upon a common axis. lastly, The beta sheets twist around the Zn^2+ ion to avoid direct contact.

Revision as of 00:36, 4 December 2021

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection></StructureSection></StructureSection>' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

This Sandbox is Reserved from September 14, 2021, through May 31, 2022, for use in the class Introduction to Biochemistry taught by User:John Means at the University of Rio Grande, Rio Grande, OH, USA. This reservation includes 5 reserved sandboxes (Sandbox Reserved 1590 through Sandbox Reserved 1594).
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • 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. For an example of a student Proteopedia page, please see Photosystem II, Tetanospasmin, or Guanine riboswitch.

Carbonic Anhydrase 1

Human Carbonic Anhydrase I

Drag the structure with the mouse to rotate

References

  1. 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
  2. Kannan KK, Ramanadham M, Jones TA. Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I. Ann N Y Acad Sci. 1984;429:49-60. PMID:6430186
   3.Badger MR, Price GD (1994). "The role of carbonic anhydrase in photosynthesis". Annu. Rev. Plant Physiol. Plant Mol. Biol. 45: 369–392. doi:10.1146/annurev.pp.45.060194.002101.
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