1BTP
UNIQUE BINDING OF A NOVEL SYNTHETIC INHIBITOR, N-[3-[4-[4-(AMIDINOPHENOXY)-CARBONYL]PHENYL]-2-METHYL-2-PROPENOYL]-N-ALLYLGLYCINE METHANESULFONATE TO BOVINE TRYPSIN, REVEALED BY THE CRYSTAL STRUCTURE OF THE COMPLEX
Summary for 1BTP
Entry DOI | 10.2210/pdb1btp/pdb |
Descriptor | BETA-TRYPSIN, CALCIUM ION (3 entities in total) |
Functional Keywords | hydrolase (serine proteinase) |
Biological source | Bos taurus (cattle) |
Cellular location | Secreted, extracellular space: P00760 |
Total number of polymer chains | 1 |
Total formula weight | 24053.03 |
Authors | Odagaki, Y.,Nakai, H.,Senokuchi, K.,Kawamura, M.,Hamanaka, N.,Nakamura, M.,Tomoo, K.,Ishida, T. (deposition date: 1995-08-11, release date: 1996-01-29, Last modification date: 2024-06-05) |
Primary citation | Odagaki, Y.,Nakai, H.,Senokuchi, K.,Kawamura, M.,Hamanaka, N.,Nakamura, M.,Tomoo, K.,Ishida, T. Unique binding of a novel synthetic inhibitor, N-[3-[4-[4-(amidinophenoxy)carbonyl]phenyl]-2-methyl-2-propenoyl]- N-allylglycine methanesulfonate, to bovine trypsin, revealed by the crystal structure of the complex. Biochemistry, 34:12849-12853, 1995 Cited by PubMed: 7548040DOI: 10.1021/bi00039a046 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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