Unknown

Dataset Information

0

FTSite: high accuracy detection of ligand binding sites on unbound protein structures.


ABSTRACT: Binding site identification is a classical problem that is important for a range of applications, including the structure-based prediction of function, the elucidation of functional relationships among proteins, protein engineering and drug design. We describe an accurate method of binding site identification, namely FTSite. This method is based on experimental evidence that ligand binding sites also bind small organic molecules of various shapes and polarity. The FTSite algorithm does not rely on any evolutionary or statistical information, but achieves near experimental accuracy: it is capable of identifying the binding sites in over 94% of apo proteins from established test sets that have been used to evaluate many other binding site prediction methods.FTSite is freely available as a web-based server at http://ftsite.bu.edu.

SUBMITTER: Ngan CH 

PROVIDER: S-EPMC3259439 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

FTSite: high accuracy detection of ligand binding sites on unbound protein structures.

Ngan Chi-Ho CH   Hall David R DR   Zerbe Brandon B   Grove Laurie E LE   Kozakov Dima D   Vajda Sandor S  

Bioinformatics (Oxford, England) 20111122 2


<h4>Motivation</h4>Binding site identification is a classical problem that is important for a range of applications, including the structure-based prediction of function, the elucidation of functional relationships among proteins, protein engineering and drug design. We describe an accurate method of binding site identification, namely FTSite. This method is based on experimental evidence that ligand binding sites also bind small organic molecules of various shapes and polarity. The FTSite algor  ...[more]

Similar Datasets

| S-EPMC7522209 | biostudies-literature
| S-EPMC7081267 | biostudies-literature
| S-EPMC2896164 | biostudies-literature
| S-EPMC3692056 | biostudies-literature
| S-EPMC2610246 | biostudies-literature
| S-EPMC4857727 | biostudies-literature
| S-EPMC3127736 | biostudies-literature
| S-EPMC2913663 | biostudies-literature
| S-EPMC3045618 | biostudies-literature
| S-EPMC4731830 | biostudies-literature