Sandbox Reserved 1630

This Sandbox is Reserved from 09/18/2020 through 03/20/2021 for use in CHEM 351 Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, IA. This reservation includes Sandbox Reserved 1628 through Sandbox Reserved 1642.

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

Protein structure

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D == Function of your Protein == the protein Epa1ACBL2Epa9–Galb1-4Glc is from Candida glabrata, which is a human fungal pathogen. function of the protein is for sugar binding. The protein is a receptor. It interacts with calcium ions, chloride ions, and sodium ions. == Biological relevance and broader implications == The protein is associated with the fungus Candida Glabrata. It is a natural yeast fungus that, if it enters the bloodstream, can have life-threatening complications for people with suppressed or weakened immune systems. The protein is important to study because it can help to determine how diverse structural hot spots effect host cell binding and ligand binding specificity. == Important amino acids == ligand are calcium, chloride, and sodium ions the ligands play a vital role in the protein because they give signals that determine the specificity of how the protein binds. the protein lacks a cataytic triad as it is a lectin and lacks enzymatic activity view of active site Structural highlights secondary structure of the protein alpha helix in red, beta strand in yellow, turn in purple, coil/loop in white The macromolecule content of the protein shows that it has a total structure weight of 29.92 kDa, the residue count is 232, and it has one unique protein chain., The A chains of the protein has a sequence length of 262. The protein has 4 helices. There are 14 parts to the beta strand. the ligands each bind to the protein through ionic bonding. Other important features the protein contains structural motifs that it has in common with other proteins of the epa family. it also shares motif loops such as CBL2, and DcisD. these are both structural loops of the protein. CBL2 is important for determining ligand binding specificity. many of the motifs are used to maintain protein structure. The protein interacts with other proteins of its protein family. these interactions are important because they allow for larger protein interactions. The dimerization interface of the protein which allows for it to make larger structure is important because it allows for the protein to stabilize its structure.

== References ==