2gdn: Difference between revisions

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[[Image:2gdn.gif|left|200px]]<br /><applet load="2gdn" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2gdn.gif|left|200px]]
caption="2gdn, resolution 1.720&Aring;" />
 
'''Crystal structure of the Mycobacterium tuberculosis beta-lactamase'''<br />
{{Structure
|PDB= 2gdn |SIZE=350|CAPTION= <scene name='initialview01'>2gdn</scene>, resolution 1.720&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6]
|GENE= blaA, blaC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
}}
 
'''Crystal structure of the Mycobacterium tuberculosis beta-lactamase'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2GDN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GDN OCA].  
2GDN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GDN OCA].  


==Reference==
==Reference==
Crystal structure and activity studies of the Mycobacterium tuberculosis beta-lactamase reveal its critical role in resistance to beta-lactam antibiotics., Wang F, Cassidy C, Sacchettini JC, Antimicrob Agents Chemother. 2006 Aug;50(8):2762-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16870770 16870770]
Crystal structure and activity studies of the Mycobacterium tuberculosis beta-lactamase reveal its critical role in resistance to beta-lactam antibiotics., Wang F, Cassidy C, Sacchettini JC, Antimicrob Agents Chemother. 2006 Aug;50(8):2762-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16870770 16870770]
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: protein structure initiative]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: psi]]
[[Category: structural genomics]]
[[Category: structural genomic]]
[[Category: tb structural genomics consortium]]
[[Category: tb structural genomics consortium]]
[[Category: tbsgc]]
[[Category: tbsgc]]


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