SMS 2.0: an updated database to study the structural plasticity of short peptide fragments in non-redundant proteins.

ABSTRACT: The function of a protein molecule is greatly influenced by its three-dimensional (3D) structure and therefore structure prediction will help identify its biological function. We have updated Sequence, Motif and Structure (SMS), the database of structurally rigid peptide fragments, by combining amino acid sequences and the corresponding 3D atomic coordinates of non-redundant (25%) and redundant (90%) protein chains available in the Protein Data Bank (PDB). SMS 2.0 provides information pertaining to the peptide fragments of length 5-14 residues. The entire dataset is divided into three categories, namely, same sequence motifs having similar, intermediate or dissimilar 3D structures. Further, options are provided to facilitate structural superposition using the program structural alignment o

SUBMITTER: Ravella D 

PROVIDER: S-EPMC5054494 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature