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(s) and Biological Relevance
Secondary structure is important in Bap1. 6MLT is composed of two major domains, the beta-prism domain and the beta-propeller domain. Yellow represents the beta-helix, with pink showing the alpha-helix, and turns in blue. Ligands are also shown in spacefill.
One of the major functions of Bap1 is it's sugar binding properties. This image shows the binding pocket on the beta-prism, which is where carbohydrates bind. The molecule is shown in spacefill and is colored based on hydrophobicity. Hydrophilic residues are shown in blue, with hydrophobic residues in red, and non charged residues in white. Lys, which makes up a large part of the binding pocket is represented in pink. The positively charged side chain on Lys makes it great for negatively charged sugars to bind to.
Broader Implications
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.
