Sandbox Reserved 1636

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 ^[1] or to the article describing Jmol ^[2] to the rescue.

Function of your Protein

[3] 

my protein is

Biological relevance and broader implications

this journal article is explaining the role of flavin FAD and how fungi uses it in the redox reaction as it takes ornithine to hydroxyornithine in order to grab the iron needed, because the bioavailability of iron in the environment is extremely limited. ^[4] this journal article also discussed Aspergillosis, which is a condition in which Aspergillus fumigatus infects the lungs causing fatal mycoses in humans as well as animals resulting in about 200,000 cases per year, in humans only, and it cases death in about half of this number. So, it is really important to study this protein and understands the mechanism with which it works in order to fight the infection and discover a new anti-fungal drug that will work better for both humans and animals.

Important amino acids

the catalytic cycle is initiated by the binding of NADPH resulting a reduction of the FAD. The most important contributions to protein ligand interactions are H-bonds and lipophilic contacts. They are driven by enthalpy and entropy. Solvation and desolvation then, affects either of . On the other hand, the protein binding site plays a big role in the binding process. Ans 323, Tyr 324, and Ser 325 are the key amino acids

are highlighted in green.

Structural highlights

secondary structure: Flavin consists of about . Flavin also has four domains. tertiary and Quaternary structures:

Other important features

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.