2po7: Difference between revisions

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[[Image:2po7.png|left|200px]]
[[Image:2po7.png|left|200px]]


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{{STRUCTURE_2po7|  PDB=2po7  |  SCENE=  }}  
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===Crystal structure of human ferrochelatase mutant with His 341 replaced by Cys===
===Crystal structure of human ferrochelatase mutant with His 341 replaced by Cys===


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{{ABSTRACT_PUBMED_17567154}}
{{ABSTRACT_PUBMED_17567154}}


==About this Structure==
==About this Structure==
[[2po7]] is a 2 chain structure with 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=2PO7 OCA].  
[[2po7]] is a 2 chain structure with 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=2PO7 OCA].  
==See Also==
*[[Ferrochelatase|Ferrochelatase]]


==Reference==
==Reference==
<ref group="xtra">PMID:17567154</ref><ref group="xtra">PMID:11175906</ref><ref group="xtra">PMID:10561552</ref><references group="xtra"/>
<ref group="xtra">PMID:017567154</ref><ref group="xtra">PMID:011175906</ref><ref group="xtra">PMID:010561552</ref><references group="xtra"/>
[[Category: Ferrochelatase]]
[[Category: Ferrochelatase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: H341c]]
[[Category: H341c]]
[[Category: Heme biosynthesis]]
[[Category: Heme biosynthesis]]
[[Category: Lyase]]
[[Category: Mature length]]
[[Category: Mature length]]
[[Category: Proteolytically processed mitochondrial inner membrane protein]]
[[Category: Proteolytically processed mitochondrial inner membrane protein]]
[[Category: Protoheme]]
[[Category: Protoheme]]

Revision as of 16:21, 30 January 2013

File:2po7.png

Template:STRUCTURE 2po7

Crystal structure of human ferrochelatase mutant with His 341 replaced by CysCrystal structure of human ferrochelatase mutant with His 341 replaced by Cys

Template:ABSTRACT PUBMED 17567154

About this StructureAbout this Structure

2po7 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1][xtra 2][xtra 3]

  1. Dailey HA, Wu CK, Horanyi P, Medlock AE, Najahi-Missaoui W, Burden AE, Dailey TA, Rose J. Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis. Biochemistry. 2007 Jul 10;46(27):7973-9. Epub 2007 Jun 14. PMID:17567154 doi:10.1021/bi700151f
  2. Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC. The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Nat Struct Biol. 2001 Feb;8(2):156-60. PMID:11175906 doi:10.1038/84152
  3. Burden AE, Wu C, Dailey TA, Busch JL, Dhawan IK, Rose JP, Wang B, Dailey HA. Human ferrochelatase: crystallization, characterization of the [2Fe-2S] cluster and determination that the enzyme is a homodimer. Biochim Biophys Acta. 1999 Nov 16;1435(1-2):191-7. PMID:10561552

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