D3PM: a comprehensive database for protein motions ranging from residue to domain.

ABSTRACT:

Background

Knowledge of protein motions is significant to understand its functions. While currently available databases for protein motions are mostly focused on overall domain motions, little attention is paid on local residue motions. Albeit with relatively small scale, the local residue motions, especially those residues in binding pockets, may play crucial roles in protein functioning and ligands binding.

Results

A comprehensive protein motion database, namely D3PM, was constructed in this study to facilitate the analysis of protein motions. The protein motions in the D3PM range from overall structural changes of macromolecule to local flip motions of binding pocket residues. Currently, the D3PM has collected 7679 proteins with overall motions and 3513 proteins with pock

SUBMITTER: Peng C 

PROVIDER: S-EPMC8845362 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature