  Membrane Proteins (MPs) account for around 15-39% of the human proteome and
assume a critical role in a vast set of cellular and physiological mechanisms,
including molecular transport, nutrient uptake, toxin and waste product
clearance, respiration, and signaling. While roughly 60% of all FDA-approved
drugs target MPs, there is a shortage of structural and biochemical data on
them mainly hindered by their localization in the lipid bilayer. We present
here MEmbrane protein dimer Novel Structure Analyser database (MENSAdb), a real
time web-application exposing a broad array of fundamental features about MPs
surface and their interfacial regions. In particular, we present conservation,
four distinctive Accessible Solvent Area (ASA) descriptors, average and
environment-specific B-factors, intermolecular contacts at 2.5 and 4.0
angstroms distance cutoffs, salt-bridges, hydrogen-bonds, hydrophobic, pi-pi
interactions, t-stacking and cation-pi interactions. Additionally, users can
closely inspect differences in values between three distinctive residues
classes: i) non-surface, ii) surface and non-interfacial and iii) interfacial.
The database is freely available at www.moreiralab.com/resources/mensadb.
