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8XNJ

Crystal structure of trypsin in-complex with arginine

Summary for 8XNJ
Entry DOI10.2210/pdb8xnj/pdb
Related8XNI
DescriptorCationic trypsin, DI(HYDROXYETHYL)ETHER, CHLORIDE ION, ... (6 entities in total)
Functional Keywordshydrolase, trypsin inhibitor, arginine, hydrolase-inhibitor complex, hydrolase/inhibitor
Biological sourceBos taurus (cattle)
Total number of polymer chains1
Total formula weight23752.05
Authors
Akbar, Z.,Ahmad, M.S. (deposition date: 2023-12-30, release date: 2024-12-04)
Primary citationAkbar, 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: 39520718
DOI: 10.1080/14786419.2024.2425793
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

243531

数据于2025-10-22公开中

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