Sandbox Reserved 1561: Difference between revisions

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<scene name='82/823085/Active_binding_sites/1'>Active Binding Sites</scene> Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller. There seems to be no catalytic triad associated within Bap1.
<scene name='82/823085/Active_binding_sites/1'>Active Binding Sites</scene> Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller. There seems to be no catalytic triad associated within Bap1.


<scene name='82/823085/Citrate_anion/1'>Citrate Anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.  
<scene name='82/823085/Citrate_anion/2'>Citrate anion</scene>The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.  


<scene name='82/823085/Asp348/1'>Asp348</scene>The beta-propeller utilizes lectins, called PropLecs, which are found in the beta-propeller folds that contain carbohydrate-binding sites. Asp348 forms essential contacts with bound carbohydrates in the beta-prism lectin domain on blade-six of the eight-bladed beta-propeller.  
<scene name='82/823085/Asp348/1'>Asp348</scene>The beta-propeller utilizes lectins, called PropLecs, which are found in the beta-propeller folds that contain carbohydrate-binding sites. Asp348 forms essential contacts with bound carbohydrates in the beta-prism lectin domain on blade-six of the eight-bladed beta-propeller.