8XNJ
Crystal structure of trypsin in-complex with arginine
Summary for 8XNJ
| Entry DOI | 10.2210/pdb8xnj/pdb |
| Related | 8XNI |
| Descriptor | Cationic trypsin, DI(HYDROXYETHYL)ETHER, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | hydrolase, trypsin inhibitor, arginine, hydrolase-inhibitor complex, hydrolase/inhibitor |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 23752.05 |
| Authors | |
| Primary citation | Akbar, Z.,Ahmad, M.S. In vitro , in silico and crystallographic-based identification of serine protease inhibitors. Nat Prod Res, :1-7, 2024 Cited by PubMed Abstract: Serine proteases are involved in various ailments, including pancreatitis, and colon cancer. Based on substrate recognition serine proteases are classified into different groups. Trypsin and trypsin-like serine proteases are among most studied group of serine proteases. Trypsin is among the chief hydrolysing enzyme involved in the pathogenesis of pancreatitis. Its inhibition can help to manage the disease. Herein, we investigated the trypsin inhibitory effect of some arginine-based small molecules, through , , and crystallographic methods. Compounds - were evaluated against bovine pancreatic trypsin (BPT). Compound was found to be active against trypsin with IC value of 247.98 ± 2.44 M. Molecular docking studies were used to investigate the binding energy and binding conformation of inhibitor. All three compounds were subjected to crystallisation with trypsin. Compounds - were successfully crystallised with BPT The crystal structures of trypsin in complexed with compounds , and were determined at 2.30 and 2.50 Å resolution, respectively. Both molecules showed their binding affinity with the active site residues of trypsin. This study will provide insight into the binding mechanism of E-64 and arginine and might be useful in designing effective inhibitors of serine proteases. PubMed: 39520718DOI: 10.1080/14786419.2024.2425793 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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