2TIO

LOW PACKING DENSITY FORM OF BOVINE BETA-TRYPSIN IN CYCLOHEXANE

2TIO の概要

• エントリーDOI: 10.2210/pdb2tio/pdb
• 分子名称: PROTEIN (BETA-TRYPSIN), CALCIUM ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: hydrolase (serine proteinase), cyclohexane, benzamidine inhibited, hydrolase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted, extracellular space: P00760
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23858.88

構造登録者

Huang, Q.,Zhu, G.,Tang, Q. (登録日: 1998-09-23, 公開日: 1998-09-30, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.93 Å)