2po5: Difference between revisions

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[[Image:2po5.jpg|left|200px]]<br /><applet load="2po5" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2po5.jpg|left|200px]]
caption="2po5, resolution 2.20&Aring;" />
 
'''Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys'''<br />
{{Structure
|PDB= 2po5 |SIZE=350|CAPTION= <scene name='initialview01'>2po5</scene>, resolution 2.20&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> and <scene name='pdbligand=CHD:CHOLIC ACID'>CHD</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= FECH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2PO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=CHD:'>CHD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2PO5 OCA].  
2PO5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA].  


==Reference==
==Reference==
Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis., Dailey HA, Wu CK, Horanyi P, Medlock AE, Najahi-Missaoui W, Burden AE, Dailey TA, Rose J, Biochemistry. 2007 Jul 10;46(27):7973-9. Epub 2007 Jun 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17567154 17567154]
Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis., Dailey HA, Wu CK, Horanyi P, Medlock AE, Najahi-Missaoui W, Burden AE, Dailey TA, Rose J, Biochemistry. 2007 Jul 10;46(27):7973-9. Epub 2007 Jun 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17567154 17567154]
[[Category: Ferrochelatase]]
[[Category: Ferrochelatase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: ferrochelatase; h263c; fe2s2 cluster; heme biosynthesis; protoheme; ferro-lyase; mature length; proteolytically processed mitochondrial inner membrane protein]]
[[Category: ferrochelatase; h263c; fe2s2 cluster; heme biosynthesis; protoheme; ferro-lyase; mature length; proteolytically processed mitochondrial inner membrane protein]]


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