Sandbox Reserved 1630

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Current revision (05:29, 8 December 2020) (edit) (undo)
 
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<scene name='86/861612/Secondary_structure/1'>secondary structure of the protein</scene> alpha helix in red, beta strand in yellow, turn in purple, coil/loop in white
<scene name='86/861612/Secondary_structure/1'>secondary structure of the protein</scene> alpha helix in red, beta strand in yellow, turn in purple, coil/loop in white
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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.
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<scene name='86/861612/Spacefill/1'>spacefill scene</scene> the spacefill view of the protein allows for a view of the intermolecular forces in the protein and to be able to see the size of the protein. Can also see where the ligands bind to the receptor areas in the protein
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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.
== Other important features ==
== Other important features ==
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</StructureSection>
</StructureSection>
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== References == <ref>PMID:32669365</ref>
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== References ==
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<ref>PMID:32669365</ref>
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Functional reprogramming of Candida glabrata epithelial adhesins: the role of conserved and variable structural motifs in ligand binding

Current revision

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

Caption for this structure

Drag the structure with the mouse to rotate

References

[1] Functional reprogramming of Candida glabrata epithelial adhesins: the role of conserved and variable structural motifs in ligand binding

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