2eql
CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION
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| , resolution 2.5Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
2EQL is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution., Tsuge H, Ago H, Noma M, Nitta K, Sugai S, Miyano M, J Biochem. 1992 Feb;111(2):141-3. PMID:1569037
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