3S0N
Crystal Structure of Human Chymase with Benzimidazolone Inhibitor
Summary for 3S0N
| Entry DOI | 10.2210/pdb3s0n/pdb |
| Descriptor | Chymase, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (5 entities in total) |
| Functional Keywords | serine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 25880.14 |
| Authors | Qian, K.C.,Farrow, N.A.,Padyana, A.K. (deposition date: 2011-05-13, release date: 2011-07-20, Last modification date: 2024-10-09) |
| Primary citation | Lo, H.Y.,Nemoto, P.A.,Kim, J.M.,Hao, M.H.,Qian, K.C.,Farrow, N.A.,Albaugh, D.R.,Fowler, D.M.,Schneiderman, R.D.,Michael August, E.,Martin, L.,Hill-Drzewi, M.,Pullen, S.S.,Takahashi, H.,De Lombaert, S. Benzimidazolone as potent chymase inhibitor: Modulation of reactive metabolite formation in the hydrophobic (P(1)) region. Bioorg.Med.Chem.Lett., 21:4533-4539, 2011 Cited by PubMed Abstract: A new class of chymase inhibitor featuring a benzimidazolone core with an acid side chain and a P(1) hydrophobic moiety is described. Incubation of the lead compound with GSH resulted in the formation of a GSH conjugate on the benzothiophene P(1) moiety. Replacement of the benzothiophene with different heterocyclic systems such as indoles and benzoisothiazole is feasible. Among the P(1) replacements, benzoisothiazole prevents the formation of GSH conjugate and an in silico analysis of oxidative potentials agreed with the experimental outcome. PubMed: 21733690DOI: 10.1016/j.bmcl.2011.05.126 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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