2q2n: Difference between revisions

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==About this Structure==
==About this Structure==
2Q2N 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=2Q2N OCA].  
2Q2N is a 1 chain 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=2Q2N OCA].  


==Reference==
==Reference==
Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues., Karlberg T, Hansson MD, Yengo RK, Johansson R, Thorvaldsen HO, Ferreira GC, Hansson M, Al-Karadaghi S, J Mol Biol. 2008 May 16;378(5):1074-83. Epub 2008 Mar 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18423489 18423489]
<ref group="xtra">PMID:18423489</ref><references group="xtra"/>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Ferrochelatase]]
[[Category: Ferrochelatase]]
[[Category: Single protein]]
[[Category: Al-Karadaghi, S.]]
[[Category: Al-Karadaghi, S.]]
[[Category: Karlberg, T.]]
[[Category: Karlberg, T.]]
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[[Category: Transferase]]
[[Category: Transferase]]


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Revision as of 10:41, 17 February 2009

File:2q2n.png

Template:STRUCTURE 2q2n

Crystal structure of Bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochlorideCrystal structure of Bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride

Template:ABSTRACT PUBMED 18423489

About this StructureAbout this Structure

2Q2N is a 1 chain structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Karlberg T, Hansson MD, Yengo RK, Johansson R, Thorvaldsen HO, Ferreira GC, Hansson M, Al-Karadaghi S. Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues. J Mol Biol. 2008 May 16;378(5):1074-83. Epub 2008 Mar 28. PMID:18423489 doi:10.1016/j.jmb.2008.03.040

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