Sandbox Reserved 1561: Difference between revisions

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<scene name='82/823085/Sodium_calcium_ion_view/1'>Sodium Calcium Ion View</scene> Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.

(All Binding Sites) Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller.

(All Binding Sites) 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.

~~There doesn’t seem to be a catalytic triad within Bap1.~~

<scene name='82/823085/Asp348_contact_formation/1'>Asp348 Contact Formation</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.

Sandbox Reserved 1561: Difference between revisions

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@@ Line 24: / Line 24: @@
 <scene name='82/823085/Sodium_calcium_ion_view/1'>Sodium Calcium Ion View</scene> Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.
-(All Binding Sites) Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller.
+(All Binding Sites) 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.
-There doesn’t seem to be a catalytic triad within Bap1.
 <scene name='82/823085/Asp348_contact_formation/1'>Asp348 Contact Formation</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.