Sandbox Reserved 1697: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 14: Line 14:


== 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 <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, 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.
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 <scene name='89/892740/Secondary_structures/1'>77% helix and 23% beta sheet</scene>, 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. <ref> PMID 33172890 </ref>


== Other important features ==
== Other important features ==

Revision as of 01:10, 8 November 2021

Text To Be Displayed

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.
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

7KIR

Inositol plyphosphate 1-phosphatase

Drag the structure with the mouse to rotate

References