Sandbox Reserved 1590

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

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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

spinqualitylabelsall models Human Carbonic Anhydrase I Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. 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 or to the article describing Jmol to the rescue. ... General Overview Human Carbonic Anhydrase I is an enzyme used to catalyze the conversion of carbon dioxide into carbonic acid then back into carbon dioxide. According to Supuran CT, Carbonic Anhydrase also plays a key role by providing CO2 transport in the blood, in turn helping respiration processes[3]. It is listed in protein data banks under the ID 2CAB. This protein is produced by the Human CA1 gene. Human Carbonic Anhydrase I was discovered in 1932 and is found within Class One of the three Carbonic Anhydrases. Class one is designated for alpha carbonic anhydrases found in mammals, class two for beta carbonic anhydrases found in plants or bacteria and finally class 3 which is gamma carbonic anhydrases found in methanogen bacteria in hot springs. Unlike many enzymes, Human Carbonic Anhydrase I can be found in many different places in the body and perform various tasks. Structure and Highlights 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 helices 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. Structural highlights This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

   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.