2ac2: Difference between revisions

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[[Image:2ac2.gif|left|200px]]<br /><applet load="2ac2" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2ac2.gif|left|200px]]
caption="2ac2, resolution 2.50&Aring;" />
 
'''Crystal structure of the Tyr13Phe mutant variant of Bacillus subtilis Ferrochelatase with Zn(2+) bound at the active site'''<br />
{{Structure
|PDB= 2ac2 |SIZE=350|CAPTION= <scene name='initialview01'>2ac2</scene>, resolution 2.50&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1]
|GENE= hemH, hemF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
}}
 
'''Crystal structure of the Tyr13Phe mutant variant of Bacillus subtilis Ferrochelatase with Zn(2+) bound at the active site'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2AC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ferrochelatase Ferrochelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.1 4.99.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AC2 OCA].  
2AC2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AC2 OCA].  


==Reference==
==Reference==
Metallation of the transition-state inhibitor N-methyl mesoporphyrin by ferrochelatase: implications for the catalytic reaction mechanism., Shipovskov S, Karlberg T, Fodje M, Hansson MD, Ferreira GC, Hansson M, Reimann CT, Al-Karadaghi S, J Mol Biol. 2005 Oct 7;352(5):1081-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16140324 16140324]
Metallation of the transition-state inhibitor N-methyl mesoporphyrin by ferrochelatase: implications for the catalytic reaction mechanism., Shipovskov S, Karlberg T, Fodje M, Hansson MD, Ferreira GC, Hansson M, Reimann CT, Al-Karadaghi S, J Mol Biol. 2005 Oct 7;352(5):1081-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16140324 16140324]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Ferrochelatase]]
[[Category: Ferrochelatase]]
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[[Category: rossman fold]]
[[Category: rossman fold]]


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