Conservation of cofactor pockets in proteins
نویسندگان
چکیده
منابع مشابه
A Comprehensive Survey of Small-Molecule Binding Pockets in Proteins
Many biological activities originate from interactions between small-molecule ligands and their protein targets. A detailed structural and physico-chemical characterization of these interactions could significantly deepen our understanding of protein function and facilitate drug design. Here, we present a large-scale study on a non-redundant set of about 20,000 known ligand-binding sites, or po...
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Voids and pockets in a protein refer to empty spaces that are enclosed by the protein molecule. Existing methods to compute, measure, and visualize the voids and pockets in a protein molecule are sensitive to inaccuracies in the empirically determined atomic radii. This paper presents a topological framework that enables robust computation and visualization of these structures. Given a fixed se...
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fPOP (footprinting Pockets Of Proteins, http://pocket.uchicago.edu/fpop/) is a relational database of the protein functional surfaces identified by analyzing the shapes of binding sites in approximately 42,700 structures, including both holo and apo forms. We previously used a purely geometric method to extract the spatial patterns of functional surfaces (split pockets) in approximately 19,000 ...
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In the current study, in order to verify the presence of bacterial Molybdenum cofactor, an indirect approach was made by showing the activity of BisC enzyme as a reporter gene. The activity of the BisC enzyme is dependent to Bis-MGD cofactor. BisC enzyme converts biotin sulfoxide to biotin under abiotic stress condition and it can also reduce TMANO and because of this property it was applied on...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations and Advances
سال: 2014
ISSN: 2053-2733
DOI: 10.1107/s2053273314084848