1aef: Difference between revisions

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New page: left|200px<br /> <applet load="1aef" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aef, resolution 2.1Å" /> '''SPECIFICITY OF LIGAN...
 
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==About this Structure==
==About this Structure==
1AEF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with HEM and 3AP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AEF OCA]].  
1AEF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with HEM and 3AP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5]]. Structure known Active Site: AVE. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AEF OCA]].  


==Reference==
==Reference==
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[[Category: transit peptide]]
[[Category: transit peptide]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:29:22 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:38:08 2007''

Revision as of 09:33, 30 October 2007

File:1aef.gif


1aef, resolution 2.1Å

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SPECIFICITY OF LIGAND BINDING TO A BURIED POLAR CAVITY AT THE ACTIVE SITE OF CYTOCHROME C PEROXIDASE (3-AMINOPYRIDINE)

OverviewOverview

Cavity complementation has been observed in many proteins, where an, appropriate small molecule binds to a cavity-forming mutant. Here, the, binding of compounds to the W191G cavity mutant of cytochrome c peroxidase, is characterized by X-ray crystallography and binding thermodynamics., Unlike cavities created by removal of hydrophobic side-chains, the W191G, cavity does not bind neutral or hydrophobic compounds, but displays a, strong specificity for heterocyclic cations, consistent with the role of, the protein to stabilize a tryptophan radical at this site. Ligand, dissociation constants for the protonated cationic state ranged from 6, microM for 2-amino-5-methylthiazole to 1 mM for neutral ligands, and, binding was associated with a large enthalpy-entropy compensation. X-ray, ... [(full description)]

About this StructureAbout this Structure

1AEF is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM and 3AP as [ligands]. Active as [Oxidoreductase], with EC number [1.11.1.5]. Structure known Active Site: AVE. Full crystallographic information is available from [OCA].

ReferenceReference

Artificial protein cavities as specific ligand-binding templates: characterization of an engineered heterocyclic cation-binding site that preserves the evolved specificity of the parent protein., Musah RA, Jensen GM, Bunte SW, Rosenfeld RJ, Goodin DB, J Mol Biol. 2002 Jan 25;315(4):845-57. PMID:11812152

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OCA