2eql

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2eql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eql OCA], [http://www.ebi.ac.uk/pdbsum/2eql PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2eql RCSB]</span>
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'''CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION'''
'''CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION'''
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[[Category: Miyano, M.]]
[[Category: Miyano, M.]]
[[Category: Tsuge, H.]]
[[Category: Tsuge, H.]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:00:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:52:34 2008''
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Revision as of 00:00, 4 May 2008

Image:2eql.jpg

Template:STRUCTURE 2eql

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


Overview

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 Structure

2EQL is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 03:00:11 2008

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