7IGC
Endothiapepsin crystal Apo17 from ECBL-96 fragment library screening campaign used for PanDDA ground state calculation
Summary for 7IGC
| Entry DOI | 10.2210/pdb7igc/pdb |
| Group deposition | Endothiapepsin vs. ECBL-96 (G_1002349) |
| Descriptor | Endothiapepsin (2 entities in total) |
| Functional Keywords | crystallographic fragment screening, endothiapepsin, ecbl-96 fragment library, hydrolase |
| Biological source | Cryphonectria parasitica (chestnut blight fungus) |
| Total number of polymer chains | 1 |
| Total formula weight | 33813.86 |
| Authors | Wollenhaupt, J.,Benz, L.S.,Jirgensons, A.,Miletic, T.,Mueller, U.,Weiss, M.S. (deposition date: 2025-06-05, release date: 2025-11-05) |
| Primary citation | Benz, L.S.,Wollenhaupt, J.,Jirgensons, A.,Miletic, T.,Mueller, U.,Weiss, M.S. From fragments to follow-ups: rapid hit expansion by making use of EU-OPENSCREEN resources. Rsc Med Chem, 2025 Cited by PubMed Abstract: Quite frequently, it is the progression of initial crystallographic fragment screening hits into more potent binders to their target, which constitutes the major bottleneck in many academic compound or drug development projects. While high quality starting points are critical to the success of a drug development project, it is equally important to have accessible pathways for further compound development. Here, we present two crystallographic fragment screening campaigns using a 96 fragment sub-selection of the European Fragment Screening Library (EFSL) provided by EU-OPENSCREEN. The two campaigns against the targets endothiapepsin and the NS2B-NS3 Zika protease, yielded hit rates of 31% and 18%, respectively. Further, we present how within the framework of the EU-OPENSCREEN European Research Infrastructure Consortium (ERIC) fast identification of follow-up compounds can be realized. With just one round of testing related compounds from the European Chemical Biology Library, two follow-up binders for each of the two targets could be identified proving the feasibility of this approach. PubMed: 41132859DOI: 10.1039/d5md00684h PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.08 Å) |
Structure validation
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