2eql
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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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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[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:52:34 2008'' |
Revision as of 23:52, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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