1DPO

STRUCTURE OF RAT TRYPSIN

1DPO の概要

• エントリーDOI: 10.2210/pdb1dpo/pdb
• 分子名称: TRYPSIN, CALCIUM ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, serine protease, digestion, pancreas, zymogen, multigene family
• 由来する生物種: Rattus rattus (black rat)
• 細胞内の位置: Secreted, extracellular space: P00763
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24423.56

構造登録者

Stroud, R.M. (登録日: 1997-03-31, 公開日: 1997-07-07, 最終更新日: 2024-11-20)

主引用文献

Earnest, T.,Fauman, E.,Craik, C.S.,Stroud, R.
1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures.
Proteins, 10:171-187, 1991

PubMed Abstract: The structure of a rat trypsin mutant [S195C] at a temperature of 120 K has been refined to a crystallographic R factor of 17.4% between 12.0 and 1.59 A and is compared with the structure of the D102N mutant at 295 K. A reduction in the unit cell dimensions in going from room temperature to low temperature is accompanied by a decrease in molecular surface area and radius of gyration. The overall structure remains similar to that at room temperature. The attainable resolution appears to be improved due to the decrease in the fall off of intensities with resolution [reduction of the temperature factor]. This decreases the uncertainty in the atomic positions and allows the localization of more protein atoms and solvent molecules in the low temperature map. The largest differences between the two models occur at residues with higher than average temperature factors. Several features can be localized in the solvent region of the 120 K map that are not seen in the 295 K map. These include several more water molecules as well as an interstitial sulfate ion and two interstitial benzamidine molecules.

PubMed: 1881877
DOI: 10.1002/prot.340100303

実験手法

X-RAY DIFFRACTION (1.59 Å)