Open-access Mustguseal platform for bioinformatic analysis in computational enzymology



Comparative analysis of homologous proteins in a functionally diverse superfamily is a valuable tool at studying structure-­function relationship, but represents a methodological challenge. We have developed an open-­access platform consisting of free on-line methods to study the structure-­function relationship in proteins, to select the most promising hot-­spots for implementation of novel functions, improvement of stability and evolvability of useful proteins/enzymes, and to design of their selective modulators.


  • The key Mustguseal web-­server can automatically collect and align thousands of homologous protein sequences and structures;

    Four sister web-­methods are available for subsequent bioinformatic analysis of the collected data:

  • the Zebra web-server to identify and prioritize conserved and specific positions in a functionally diverse superfamily and to select hot-spots for rational design of the query protein;

  • the pocketZebra web-server to identify and rank binding sites in proteins by their functional significance and to select particular positions in the structure important for selective binding of substrates/inhibitors/effectors;

  • the visualCMAT web-server to select and interpret correlated mutations/co-­evolving residues in protein structures;

  • the Yosshi web­-server to classify and study disulfide bonds in protein families as well as to select hot­-spots for disulfide engineering.


Integration of these bioinformatic web-tools provides an out-­of­-the­box easy­-to-­use solution, first of its kind, to systematically analyze all the available sequence and structural data related to a protein superfamily, thus promoting the value of bioinformatics for protein engineering and drug discovery.




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FEBS 2019 Congress Poster: D. Suplatov, Y. Sharapova, D. Timonina, E. Schmalhausen, K. Fesko, N. Popova, V. Muronets, V. Voevodin, V. Švedas (2019) Open­access Mustguseal platform for bioinformatic analysis in computational enzymology. FEBS Congress 2019, poster: [download]


FEBS 2019 Congress Talk: Sharapova Y., Suplatov D., Timonina D., Schmalhausen E., Fesko K., Muronets V., Voevodin V., Svedas V. (2019) Assessing protein flexibility in computational enzymology: conformational sampling or 3D-motif analysis? FEBS Congress 2019, abstract: [view]

A brief overview of the Mustguseal platform:

Download PDF file (2.3 MB)


This work is being funded by the Russian Foundation for Basic Research [#18-­29-­13060] and carried out using the HPC computing resources at the Lomonosov Moscow State University supported by the project RFMEFI62117X0011.