Welcome to the Protein Ensemble Database!

What is an IDP?

Structural heterogeneity is intimate to the functioning of many proteins and thus describing a protein with a single native structure is often insufficient to elucidate its function. In particular, intrinsically disordered proteins (IDPs) can only be approached by solution techniques and described as structural ensembles. The same is true for multidomain proteins that have disordered linkers. Apparently, the ensemble representations of these proteins carry essential function-related information, yet they have not been available until now.

Read more about IDPs...

What is an ensemble?

The goal of PED is to serve as an openly accessible database for the deposition of structural information on IDP- and denatured protein ensembles based on Nuclear Magnetic Resonance (NMR) and Small-angle X-ray Scattering (SAXS) data. We are also hosting purely computational models, typically from Molecular Dynamics (MD) simulations. The deposition of structural coordinates as well as primary data can be used for evaluating and re-calculating the ensembles, thus supporting the evolution of new modeling methods leading to much improved skills of connecting "unstructure" with function.

Read more about ensembles...

Latest news

Data submission is temporarily suspended until further notice

PED stores 25473 protein structures of 60 ensembles in 24 entries as of 06/26/2017 12:16:18 pm
For citing PED, please refer to: Mihaly Varadi, Simone Kosol, Pierre Lebrun, Erica Valentini, Martin Blackledge, A. Keith Dunker, Isabella C. Felli, Julie D. Forman-Kay, Richard W. Kriwacki, Roberta Pierattelli, Joel Sussman, Dmitri I. Svergun, Vladimir N. Uversky, Michele Vendruscolo, David Wishart, Peter E. Wright and Peter Tompa 'pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins' Nucleic Acids Res. 2014 Jan (Database issue); Epub 2013 Oct 29.
Maintained by the Tompa Lab at VIB SBRC
Originally developed by Mihaly Varadi