1hqw: Difference between revisions
New page: left|200px<br /><applet load="1hqw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hqw, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1hqw.gif|left|200px]]<br /><applet load="1hqw" size=" | [[Image:1hqw.gif|left|200px]]<br /><applet load="1hqw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1hqw, resolution 2.40Å" /> | caption="1hqw, resolution 2.40Å" /> | ||
'''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== | ||
The X-ray structure analysis of a cross-linked crystal of concanavalin A | 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== | ||
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:// | 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]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:57 2008'' |
Revision as of 14:03, 21 February 2008
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CRYSTAL STRUCTURE OF THE COMPLEX OF CONCANAVALIN A WITH A TRIPEPTIDE YPY
OverviewOverview
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 StructureAbout this Structure
1HQW is a Single protein structure of sequence from Canavalia ensiformis with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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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