2EQL

CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION

2EQL の概要

• エントリーDOI: 10.2210/pdb2eql/pdb
• 分子名称: HORSE MILK LYSOZYME (1 entity in total)
• 機能のキーワード: hydrolase(o-glycosyl)
• 由来する生物種: Equus caballus (horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14673.63

構造登録者

Tsuge, H.,Ago, H.,Miyano, M. (登録日: 1994-05-27, 公開日: 1994-07-31, 最終更新日: 2024-11-20)

主引用文献

Tsuge, H.,Ago, H.,Noma, M.,Nitta, K.,Sugai, S.,Miyano, M.
Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution.
J.Biochem.(Tokyo), 111:141-143, 1992

PubMed Abstract: The crystal structure of a calcium binding equine lysozyme has been determined at 2.5 A resolution by means of molecular replacement. The energy minimized equine lysozyme as the starting model, was refined with the molecular dynamics program, X-PLOR, and the R factor of the current model was found to be 24% without any water molecules. The conformation of the calcium binding loop is similar to that of alpha-lactalbumin. The profiles of backbone atomic displacements throughout the lysozyme and alpha-lactalbumin superfamilies are comparable as well as their homologous tertiary structures.

PubMed: 1569037

実験手法

X-RAY DIFFRACTION (2.5 Å)