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1hqw

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(New page: 200px<br /><applet load="1hqw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hqw, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1hqw.gif|left|200px]]<br /><applet load="1hqw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hqw, resolution 2.40&Aring;" />
caption="1hqw, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF THE COMPLEX OF CONCANAVALIN A WITH A TRIPEPTIDE YPY'''<br />
'''CRYSTAL STRUCTURE OF THE COMPLEX OF CONCANAVALIN A WITH A TRIPEPTIDE YPY'''<br />
==Overview==
==Overview==
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The X-ray structure analysis of a cross-linked crystal of concanavalin A, soaked with the tripeptide molecule as the probe molecule showed electron, density corresponding to full occupation in the binding pocket. The site, lies on the surface of concanavalin A and is surrounded by three, symmetry-related molecules. The crystal structure of the tripeptide, complex was refined at 2.4-A resolution to an R-factor of 17.5%, (Rfree, factor of 23.7%), with an RMS deviation in bond distances of 0.01 A. The, model includes all 237 residue of concanavalin A, 1 manganese ion, 1, calcium ion, 161 water molecules, 1 glutaraldehyde molecule, and 1, tripeptide molecule. This X-ray structure analysis also provides an, approach to mapping the binding surface of crystalline protein with a, probe molecule that is dissolved in a mixture of organic solvent with, water or in neat organic solvent but is hardly dissolved in aqueous, solution.
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The X-ray structure analysis of a cross-linked crystal of concanavalin A soaked with the tripeptide molecule as the probe molecule showed electron density corresponding to full occupation in the binding pocket. The site lies on the surface of concanavalin A and is surrounded by three symmetry-related molecules. The crystal structure of the tripeptide complex was refined at 2.4-A resolution to an R-factor of 17.5%, (Rfree factor of 23.7%), with an RMS deviation in bond distances of 0.01 A. The model includes all 237 residue of concanavalin A, 1 manganese ion, 1 calcium ion, 161 water molecules, 1 glutaraldehyde molecule, and 1 tripeptide molecule. This X-ray structure analysis also provides an approach to mapping the binding surface of crystalline protein with a probe molecule that is dissolved in a mixture of organic solvent with water or in neat organic solvent but is hardly dissolved in aqueous solution.
==About this Structure==
==About this Structure==
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1HQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with MN, CA and PTD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HQW OCA].
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1HQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=PTD:'>PTD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQW OCA].
==Reference==
==Reference==
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[[Category: beta sheets]]
[[Category: beta sheets]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:45:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:57 2008''

Revision as of 11:03, 21 February 2008

Image:1hqw.gif

1hqw, resolution 2.40Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE COMPLEX OF CONCANAVALIN A WITH A TRIPEPTIDE YPY

Overview

The X-ray structure analysis of a cross-linked crystal of concanavalin A soaked with the tripeptide molecule as the probe molecule showed electron density corresponding to full occupation in the binding pocket. The site lies on the surface of concanavalin A and is surrounded by three symmetry-related molecules. The crystal structure of the tripeptide complex was refined at 2.4-A resolution to an R-factor of 17.5%, (Rfree factor of 23.7%), with an RMS deviation in bond distances of 0.01 A. The model includes all 237 residue of concanavalin A, 1 manganese ion, 1 calcium ion, 161 water molecules, 1 glutaraldehyde molecule, and 1 tripeptide molecule. This X-ray structure analysis also provides an approach to mapping the binding surface of crystalline protein with a probe molecule that is dissolved in a mixture of organic solvent with water or in neat organic solvent but is hardly dissolved in aqueous solution.

About this Structure

1HQW is a Single protein structure of sequence from Canavalia ensiformis with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the complex of concanavalin A and tripeptide., Zhang Z, Qian M, Huang Q, Jia Y, Tang Y, Wang K, Cui D, Li M, J Protein Chem. 2001 Jan;20(1):59-65. PMID:11330349

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