2bls: Difference between revisions

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[[Image:2bls.jpg|left|200px]]<br /><applet load="2bls" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2bls.jpg|left|200px]]
caption="2bls, resolution 2.0&Aring;" />
 
'''AMPC BETA-LACTAMASE FROM ESCHERICHIA COLI'''<br />
{{Structure
|PDB= 2bls |SIZE=350|CAPTION= <scene name='initialview01'>2bls</scene>, resolution 2.0&Aring;
|SITE= <scene name='pdbsite=ACB:Enzyme+Active+Site'>ACB</scene> and <scene name='pdbsite=ACT:Enzyme+Active+Site'>ACT</scene>
|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= AMPC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''AMPC BETA-LACTAMASE FROM ESCHERICHIA COLI'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2BLS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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] Known structural/functional Sites: <scene name='pdbsite=ACB:Enzyme+Active+Site'>ACB</scene> and <scene name='pdbsite=ACT:Enzyme+Active+Site'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BLS OCA].  
2BLS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BLS OCA].  


==Reference==
==Reference==
Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design., Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ, Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9819201 9819201]
Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design., Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ, Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9819201 9819201]
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: serine hydrolase]]
[[Category: serine hydrolase]]


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