MensaDB
Membrane protein dimer structure analysis: an open, interactive platform.
15โ39%
of the human proteome are MPs
~60%
of FDA-approved drugs target MPs
First
dimer interface analysis database
Membrane proteins (MPs) are central to a vast range of cellular processes, from molecular transport and nutrient uptake to signalling and drug interaction, yet remain structurally undercharacterised due to the challenges of their lipid bilayer environment.
MENSAdb addresses this gap as the first database to report a systematic structural and physico-chemical analysis of a curated collection of membrane protein dimer structures. Interface residues are characterised across multiple descriptors including accessible surface area, conservation, B-factor, and a full suite of non-covalent interactions, all computed in real time and presented in an interactive, user-friendly format.
Available Features
- ASA & ฮASA
- Jensen-Shannon conservation
- H-bond & salt bridge contacts
- ฯ-stacking interactions
- B-factor analysis
- PSSM / BLOSUM62
- Data export
Explore the database interactively! Browse dimer interfaces, filter by amino-acid type & export structural data all in your browser: