Sandbox Reserved 1566

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This image depicts the binding pocket at the top of the β-prism domain (the smaller complex). The image was put into spacefill so it is easier to see the pocket and identify steric significance.
This image depicts the binding pocket at the top of the β-prism domain (the smaller complex). The image was put into spacefill so it is easier to see the pocket and identify steric significance.
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<scene name='82/823090/Space_fill/3'>Hydrophilic Amino Acids Important in Carbohydrate Binding</scene>
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<scene name='82/823090/Space_fill/3'>Hydrophilic Amino Acids Important in Carbohydrate and Citrate Binding</scene>
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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 lime green. The positively charged side chain on Lys makes it great for negatively charged sugars to bind to.
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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 lime green. The positively charged side chain on Lys makes it great for negatively charged sugars (and citrate) to bind to.
<scene name='82/823090/Asp_348/1'>Asp 348 Important Residue in Citrate Orientation and Sugar Binding</scene>
<scene name='82/823090/Asp_348/1'>Asp 348 Important Residue in Citrate Orientation and Sugar Binding</scene>
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<scene name='82/823090/Important_aas/1'>Amino Acids Involved in Citrate Interactions</scene>
<scene name='82/823090/Important_aas/1'>Amino Acids Involved in Citrate Interactions</scene>
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There are six essential amino acids involved in the binding of citrate. These six amino acids include Gly 344, Ala 345, Val 346, Lys 501, Asp 348, and His 500. Gly 344, Ala 345, Val 346, Lys 501 all interact with citrate via hydrogen bonding, while Asp 348 and His 500 interact via van der Waals interactions. The amino acids are shown in CPK to highlight properties that correspond with hydrogen bonding.
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There are six essential amino acids involved in the binding of citrate. These six amino acids include Gly 344, Ala 345, Val 346, Lys 501, Asp 348, and His 500. Gly 344, Ala 345, Val 346, Lys 501 all interact with citrate via hydrogen bonding, while Asp 348 and His 500 interact via van der Waals interactions. The amino acids are shown in CPK to highlight properties that correspond with hydrogen bonding. Citrate molecules bind at the carbohydrate-binding site just as carbohydrates do.

Revision as of 02:42, 1 December 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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6MLT Protein Bap1

Caption for this structure

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References


[1]

[2]

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