4GCH
STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN
Summary for 4GCH
| Entry DOI | 10.2210/pdb4gch/pdb |
| Descriptor | GAMMA-CHYMOTRYPSIN A, 3-(4-DIETHYLAMINO-2-HYDROXY-PHENYL)-2-METHYL-PROPIONIC ACID, ... (5 entities in total) |
| Functional Keywords | hydrolase (serine proteinase) |
| Biological source | Bos taurus (cattle) More |
| Cellular location | Secreted, extracellular space: P00766 P00766 P00766 |
| Total number of polymer chains | 3 |
| Total formula weight | 25511.87 |
| Authors | Stoddard, B.L.,Ringe, D.,Petsko, G.A. (deposition date: 1989-09-25, release date: 1990-10-15, Last modification date: 2024-11-13) |
| Primary citation | Stoddard, B.L.,Bruhnke, J.,Porter, N.,Ringe, D.,Petsko, G.A. Structure and activity of two photoreversible cinnamates bound to chymotrypsin. Biochemistry, 29:4871-4879, 1990 Cited by PubMed Abstract: The serine protease gamma-chymotrypsin was covalently inhibited with two different photoreversible cinnamate compounds, and the structures of the resulting complexes were determined to 1.9-A resolution. The inhibitors show different kinetics of binding, inhibition, and nonphotochemical deacylation relative to each other in solution activity assays. The crystal structures of the enzyme-cinnamate complexes show that both compounds acylate serine 195 and that the two molecules are bound in similar nonproductive conformations which have drastic effects on their ability to turn over. Substitution of a diethylamino group on the para position of the cinnamate ring causes a 1000-fold increase in the thermal stability of the inhibitor toward hydrolysis and deacylation. PubMed: 2364065DOI: 10.1021/bi00472a017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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