2tio

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Revision as of 11:57, 21 November 2007

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spinqualitylabelsall models 2tio, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

LOW PACKING DENSITY FORM OF BOVINE BETA-TRYPSIN IN CYCLOHEXANE

Overview

Two orthorhombic forms (Vm values are 2.3 and 3.0 A3/Da) of bovine, beta-trypsin crystals in neat cyclohexane were determined to 1.93 A, resolution, by X-ray diffraction. Both structures in organic solvent are, similar to those in aqueous solution. In the high packing density form, one cyclohexane molecule is found in a hydrophobic site near the active, center. One sulfate locates at the active site with hydrogen or salt bond, to the Ser-His catalytic diad, and five more sulfates bind on the, molecular surface. The conformation of the side chains near the sulfates, changed greatly. In the low packing density form, one cyclohexane and, three sulfates are found. In both structures, one benzamidine molecule, locates at the hydrophobic pocket of the active center. Most water, molecules on the enzyme surface are retained except some with high, temperature factors.

About this Structure

2TIO is a Single protein structure of sequence from Bos taurus with CA, SO4, BEN and HEX as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

Reference

X-ray studies on two forms of bovine beta-trypsin crystals in neat cyclohexane., Zhu G, Huang Q, Wang Z, Qian M, Jia Y, Tang Y, Biochim Biophys Acta. 1998 Dec 8;1429(1):142-50. PMID:9920392

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