2eql
From Proteopedia
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| - | [[Image:2eql.jpg|left|200px]] | + | [[Image:2eql.jpg|left|200px]] |
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| - | '''CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 2eql |SIZE=350|CAPTION= <scene name='initialview01'>2eql</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2EQL is a [ | + | 2EQL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EQL OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1569037 1569037] |
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:43:17 2008'' |
Revision as of 14:43, 20 March 2008
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| 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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