Sandbox Reserved 434: Difference between revisions
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===Binding Interactions=== | ===Binding Interactions=== | ||
<scene name='Sandbox_Reserved_434/Scissile_bond_25/4'>The green is residue number 25</scene> | <scene name='Sandbox_Reserved_434/Scissile_bond_25/4'>The green is residue number 25</scene> | ||
In the first half of a two-step reaction, the motif uses Pb2+ to cleave the phosphodiester backbone of the substrate strand, yielding a free 5ʹ′-hydroxyl and a 2ʹ′,3ʹ′-cyclic phosphodiester as products, which is analogous to the activity catalyzed by naturally occurring small ribozymes such as the hammerhead and hairpin. The cyclic phosphate is hydrolyzed subsequently to produce a 3ʹ′-phosphate in a manner similar to that of protein ribonuclease A. | |||
===Additional Features=== | ===Additional Features=== | ||
Revision as of 04:04, 5 March 2012
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
Leadzyme, 1nuv
|
Introduction
Active site. Residues 18-30,39-49.
Overall Structure
Binding Interactions
The green is residue number 25 In the first half of a two-step reaction, the motif uses Pb2+ to cleave the phosphodiester backbone of the substrate strand, yielding a free 5ʹ′-hydroxyl and a 2ʹ′,3ʹ′-cyclic phosphodiester as products, which is analogous to the activity catalyzed by naturally occurring small ribozymes such as the hammerhead and hairpin. The cyclic phosphate is hydrolyzed subsequently to produce a 3ʹ′-phosphate in a manner similar to that of protein ribonuclease A.
Additional Features
Credits
Introduction - name of team member
Overall Structure - name of team member
Drug Binding Site - name of team member
Additional Features - Tom Foley
