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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 DOI10.2210/pdb1btp/pdb
DescriptorBETA-TRYPSIN, CALCIUM ION (3 entities in total)
Functional Keywordshydrolase (serine proteinase)
Biological sourceBos taurus (cattle)
Cellular locationSecreted, extracellular space: P00760
Total number of polymer chains1
Total formula weight24053.03
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: 2011-07-13)
Primary citationOdagaki, 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: 7548040
DOI: 10.1021/bi00039a046
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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