2EQL

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

Summary for 2EQL

• Entry DOI: 10.2210/pdb2eql/pdb
• Descriptor: HORSE MILK LYSOZYME (1 entity in total)
• Functional Keywords: hydrolase(o-glycosyl)
• Biological source: Equus caballus (horse)
• Total number of polymer chains: 1
• Total formula weight: 14673.63

Authors

Tsuge, H.,Ago, H.,Miyano, M. (deposition date: 1994-05-27, release date: 1994-07-31, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)