Unknown

Dataset Information

0

XSuLT: a web server for structural annotation and representation of sequence-structure alignments.


ABSTRACT: The web server XSuLT, an enhanced version of the protein alignment annotation program JoY, formats a submitted multiple-sequence alignment using three-dimensional (3D) structural information in order to assist in the comparative analysis of protein evolution and in the optimization of alignments for comparative modelling and construct design. In addition to the features analysed by JoY, which include secondary structure, solvent accessibility and sidechain hydrogen bonds, XSuLT annotates each amino acid residue with residue depth, chain and ligand interactions, inter-residue contacts, sequence entropy, root mean square deviation and secondary structure and disorder prediction. It is also now integrated with built-in 3D visualization which interacts with the formatted alignment to facilitate inspection and understanding. Results can be downloaded as stand-alone HTML for the formatted alignment and as XML with the underlying annotation data. XSuLT is freely available at http://structure.bioc.cam.ac.uk/xsult/.

SUBMITTER: Ochoa-Montano B 

PROVIDER: S-EPMC5793734 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

XSuLT: a web server for structural annotation and representation of sequence-structure alignments.

Ochoa-Montaño Bernardo B   Blundell Tom L TL  

Nucleic acids research 20170701 W1


The web server XSuLT, an enhanced version of the protein alignment annotation program JoY, formats a submitted multiple-sequence alignment using three-dimensional (3D) structural information in order to assist in the comparative analysis of protein evolution and in the optimization of alignments for comparative modelling and construct design. In addition to the features analysed by JoY, which include secondary structure, solvent accessibility and sidechain hydrogen bonds, XSuLT annotates each am  ...[more]

Similar Datasets

| S-EPMC2447800 | biostudies-literature
| S-EPMC4086088 | biostudies-literature
| S-EPMC1933189 | biostudies-literature
| S-EPMC6031051 | biostudies-literature
| S-EPMC2248443 | biostudies-literature
| S-EPMC7319579 | biostudies-literature
| S-EPMC8262756 | biostudies-literature
| S-EPMC4987884 | biostudies-other
| S-EPMC1933127 | biostudies-literature
| S-EPMC10623726 | biostudies-literature