EnzyMM - The Enzyme-Motif-Miner
EnzyMM identifies catalytic motifs in protein structures.
Search for any conserved arrangement of catalytic residues found in our M-CSA
derived libary of 6780 templates representing a majority of M-CSA mechanisms
in composite sub-patterns and different conformations.
Enter a PDB ID or a UniProt ID (to search
the Alphafold Database) below or upload your own structure to find, analyze
and view matching catalytic motifs.
⚙️ Version Information:
-
EnzyMM
version: 0.3.1| 📚 EnzyMM Documentation -
PyJess
version: 0.9.1| 📚 PyJess Documentation
🔖 Citations
If you find EnzyMM useful, please cite:
- EnzyMM as: Hackett R., Riziotis I., Larralde M., Zeller G., Thornton J.M. (2025). EnzyMM: A paper I am yet to publish. Stay tuned!. DOI: 10.xxxx/enzymm.2025.xxxx (placeholder)
- Mechanism and Catalytic Site Atlas (M-CSA) as: Ribeiro A.J.M. et al. (2017), Nucleic Acids Res, 46, D618–D623. Mechanism and Catalytic Site Atlas (M-CSA): a database of enzyme reaction mechanisms and active sites. DOI: 10.1093/nar/gkx1012. PMID: 29106569.
Development Credits:
EnzyMM is developed by Raymund Hackett and the Zeller Group at the Leiden University Medical Center in Leiden, the Netherlands, with continuing support from the Thornton Group at the EMBL-EBI in Hinxton, UK.
We would like to specifically credit Ioannis Riziotis, Martin Larralde, Antonio Ribeiro, Jonathan Barker, Georg Zeller, and Janet Thornton for their amazing support.
EnzyMM is developed by Raymund Hackett and the Zeller Group at the Leiden University Medical Center in Leiden, the Netherlands, with continuing support from the Thornton Group at the EMBL-EBI in Hinxton, UK.
We would like to specifically credit Ioannis Riziotis, Martin Larralde, Antonio Ribeiro, Jonathan Barker, Georg Zeller, and Janet Thornton for their amazing support.