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- W2079672600 abstract "Locating functionally important protein surfaces and identifying the catalytic site residues are critical for studying enzyme functions. Here, we present a method for predicting and characterizing catalytic sites of enzymes that is fold-independent. By extract atomic patterns of catalytic residues in surface pockets computed geometrically, we develop a library of atomic patterns on protein functional surfaces of ca 700 structures. Together with propensities of secondary structures and residue occurrence in active sites, we develop a method to identify functionally important surfaces on protein structures and to locate key residues. We discuss application of our methods to amylase, dioxygenase, deaminase, dehalogenase, and hydratase. A large scale cross-validated prediction study shows that our method is sensitive and specific. Our method can used to study enzyme function, drug design, and engineering novel biochemical function." @default.
- W2079672600 created "2016-06-24" @default.
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- W2079672600 date "2007-02-09" @default.
- W2079672600 modified "2023-09-23" @default.
- W2079672600 title "Predicting Enzyme Functional Surfaces and Locating Key Residues Automatically from Structures" @default.
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- W2079672600 doi "https://doi.org/10.1007/s10439-006-9241-2" @default.
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