Team:WLC-Milwaukee/Modeling

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<h2>yesZ</h2>The Beta-Galactosidase yesZ is globular and has three aspects that are important to its function. It contains a zinc ion binding site at the C residues 153, 155, and 158 in yellow. The putative nucleophile and acid base cleavage sites are at the E residues 155 and 296 in red. The active site where substrate binding occurs is through the amino acid residue sequence ETSPSYAASL from residues 296- 305.
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<img src="https://static.igem.org/mediawiki/2013/6/6d/WLC-YesZmod.png" width="450">
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<img src="https://static.igem.org/mediawiki/2013/e/e3/WLC-Bglsmod.png" width="450">
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<h2>bglS</h2>
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The endo-1,3-1,4-glucanase bglS is a globular protein that that has two residues of interest. The putative nucleophile and acid-base cleavage sites at the E residues 133 and 137 highlighted in red.
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<h2>xynA</h2>
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The endo-1,4-beta-xylanase xynA is a globular protein that has two residues of interest the nucleophile and acid-base cleavage sites at the E residues 78 and 172 highlighted in red.
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<img src="https://static.igem.org/mediawiki/2013/7/72/WLC-XynAmod.jpg" width="450">
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If you choose to include a '''Modeling''' page, please write about your modeling adventures here.  This is not necessary but it may be a nice list to include.
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Revision as of 16:50, 27 September 2013

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yesZ

The Beta-Galactosidase yesZ is globular and has three aspects that are important to its function. It contains a zinc ion binding site at the C residues 153, 155, and 158 in yellow. The putative nucleophile and acid base cleavage sites are at the E residues 155 and 296 in red. The active site where substrate binding occurs is through the amino acid residue sequence ETSPSYAASL from residues 296- 305.

bglS

The endo-1,3-1,4-glucanase bglS is a globular protein that that has two residues of interest. The putative nucleophile and acid-base cleavage sites at the E residues 133 and 137 highlighted in red.

xynA

The endo-1,4-beta-xylanase xynA is a globular protein that has two residues of interest the nucleophile and acid-base cleavage sites at the E residues 78 and 172 highlighted in red.

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