2TIO

LOW PACKING DENSITY FORM OF BOVINE BETA-TRYPSIN IN CYCLOHEXANE

Summary for 2TIO

• Entry DOI: 10.2210/pdb2tio/pdb
• Descriptor: PROTEIN (BETA-TRYPSIN), CALCIUM ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: hydrolase (serine proteinase), cyclohexane, benzamidine inhibited, hydrolase
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted, extracellular space: P00760
• Total number of polymer chains: 1
• Total formula weight: 23858.88

Authors

Huang, Q.,Zhu, G.,Tang, Q. (deposition date: 1998-09-23, release date: 1998-09-30, Last modification date: 2024-11-20)

Primary citation

Zhu, G.,Huang, Q.,Wang, Z.,Qian, M.,Jia, Y.,Tang, Y.
X-ray studies on two forms of bovine beta-trypsin crystals in neat cyclohexane.
Biochim.Biophys.Acta, 1429:142-150, 1998

PubMed Abstract: 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.

PubMed: 9920392
DOI: 10.1016/S0167-4838(98)00226-X

Experimental method

X-RAY DIFFRACTION (1.93 Å)