1jrs
From Proteopedia
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HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN
Overview
Three-dimensional structures of trypsin with the reversible inhibitor, leupeptin have been determined in two different crystal forms. The first, structure was determined at 1.7 A resolution with R-factor = 17.7% in the, trigonal crystal space group P3(1)21, with unit cell dimensions of a = b =, 55.62 A, c = 110.51 A. The second structure was determined at a resolution, of 1.8 A with R-factor = 17.5% in the orthorhombic space group, P2(1)2(1)2(1), with unit cell dimensions of a = 63.69 A, b = 69.37 A, c =, 63.01 A. The overall protein structure is very similar in both crystal, forms, with RMS difference for main-chain atoms of 0.27 A. The leupeptin, backbone forms four hydrogen bonds with trypsin and a fifth hydrogen bond, interaction is mediated by a water molecule. The aldehyde carbonyl of, leupeptin forms a covalent bond of 1.42 A length with side-chain oxygen of, Ser-195 in the active site. The reaction of trypsin with leupeptin, proceeds through the formation of stable tetrahedral complex in which the, hemiacetal oxygen atom is pointing out of the oxyanion hole and forming a, hydrogen bond with His-57.
About this Structure
1JRS is a Single protein structure of sequence from Bos taurus with CA and ACE as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
Two crystal structures of the leupeptin-trypsin complex., Kurinov IV, Harrison RW, Protein Sci. 1996 Apr;5(4):752-8. PMID:8845765
Page seeded by OCA on Tue Nov 20 18:31:37 2007
Categories: Bos taurus | Single protein | Trypsin | Harrison, R.W. | Kurinov, I.V. | ACE | CA | Digestion | Hydrolase | Pancreas | Serine protease | Zymogen
