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.

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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 == important amino acids are Asp, His, Asn, Lys, == Structural highlights == 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. there are three unit cell lengths, a's is 74.22, b's is 104.14 and c's is 69.09. all have an angle of 90 degrees.

== References == D. (2020, April 21). Functional reprogramming of Candida glabrata epithelial adhesins: The role of conserved and variable structural motifs in ligand binding.