Sandbox Reserved 1566
From Proteopedia
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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. | 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. | ||
| - | <scene name='82/823090/Space_fill/ | + | <scene name='82/823090/Space_fill/3'>Hydrophilic Amino Acids Important in Carbohydrate Binding</scene> |
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. | 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. | ||
Revision as of 23:41, 30 November 2019
| This Sandbox is Reserved from Aug 26 through Dec 12, 2019 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1556 through Sandbox Reserved 1575. |
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Stucture of 6MLT
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.
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