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PDBsum entry 1tio
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References listed in PDB file
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Key reference
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Title
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X-Ray studies on two forms of bovine beta-Trypsin crystals in neat cyclohexane.
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Authors
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G.Zhu,
Q.Huang,
Z.Wang,
M.Qian,
Y.Jia,
Y.Tang.
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Ref.
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Biochim Biophys Acta, 1998,
1429,
142-150.
[DOI no: ]
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PubMed id
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Abstract
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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.
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