Sandbox Reserved 1630: Difference between revisions

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== Structural highlights ==  
== Structural highlights ==  
<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
<scene name='86/861612/Spacefill/1'>spacefill scene</scene>
 
<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
 
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.  
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.  


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</StructureSection>
</StructureSection>
== References == <ref>PMID:32669365</ref>
== References ==  
<ref>PMID:32669365</ref>
Functional reprogramming of Candida glabrata epithelial adhesins: the role of conserved and variable structural motifs in ligand binding
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