7H6B
THE 2.17 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH methyl 4-[(5-fluoro-3-methyl-1-benzothiophen-2-yl)sulfonylamino]-3-methylsulfonylbenzoate (TOA EIYO INHIBITOR)
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Summary for 7H6B
| Entry DOI | 10.2210/pdb7h6b/pdb |
| Group deposition | A set of chymase crystal structures for D3R plus two CatG off-target structures (G_1002292) |
| Descriptor | Chymase, methyl 4-(5-fluoro-3-methyl-1-benzothiophene-2-sulfonamido)-3-(methanesulfonyl)benzoate (3 entities in total) |
| Functional Keywords | human chymase, serine proteinase, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 25508.42 |
| Authors | Banner, D.W.,Benz, J.M.,Schlatter, D.,Hilpert, H. (deposition date: 2024-04-19, release date: 2025-03-05, Last modification date: 2026-03-04) |
| Primary citation | Tosstorff, A.,Rudolph, M.G.,Benz, J.,Kuhn, B.,Kramer, C.,Sharpe, M.,Huang, C.Y.,Metz, A.,Hazemann, J.,Ritz, D.,Sweeney, A.M.,Gilson, M.K. The CASP 16 Experimental Protein-Ligand Datasets. Proteins, 94:79-85, 2026 Cited by PubMed Abstract: This paper presents the experimental protein-ligand datasets used as benchmarks in the CASP 16 blind prediction experiment-the first CASP round to incorporate targets from pharmaceutical discovery projects. We have assembled and characterized protein-ligand complexes for four proteins that are known or candidate drug targets: human chymase, human cathepsin G, human autotaxin, and the SARS-CoV-2 main protease. The collection encompasses over 200 co-crystal structures at resolutions better than 2.7 Å, paired with binding affinity measurements for approximately 160 compounds covering a broad affinity range (nanomolar to high micromolar). These data enabled the CASP16 pose-prediction and affinity-prediction challenges. Many systems feature potentially challenging characteristics, including chymase's electropositive surface and acidic ligands, which require proper handling of titratable ligand groups; autotaxin complexes with and without zinc coordination; and a SARS-CoV-2 protease crystal form exhibiting an unusually open active site conformation. We describe the experimental approaches-from protein production and crystallization to binding assay development-that yielded these reference data. Contributed by scientists at F. Hoffmann-La Roche and Idorsia Pharmaceuticals, these datasets represent actual drug discovery projects and therefore provide a realistic testbed for assessing how computational methods perform on pharmaceutically relevant targets. An accompanying paper in the present special journal issue provides a comprehensive assessment of the pose and affinity predictions for these pharmaceutical protein-ligand systems. PubMed: 41040057DOI: 10.1002/prot.70053 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.17 Å) |
Structure validation
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