2ac2

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[[Image:2ac2.png|left|200px]]
[[Image:2ac2.png|left|200px]]
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{{STRUCTURE_2ac2| PDB=2ac2 | SCENE= }}
{{STRUCTURE_2ac2| PDB=2ac2 | SCENE= }}
===Crystal structure of the Tyr13Phe mutant variant of Bacillus subtilis Ferrochelatase with Zn(2+) bound at the active site===
===Crystal structure of the Tyr13Phe mutant variant of Bacillus subtilis Ferrochelatase with Zn(2+) bound at the active site===
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{{ABSTRACT_PUBMED_16140324}}
{{ABSTRACT_PUBMED_16140324}}
==About this Structure==
==About this Structure==
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2AC2 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=2AC2 OCA].
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[[2ac2]] is a 1 chain structure with 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==
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<ref group="xtra">PMID:16140324</ref><references group="xtra"/>
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<ref group="xtra">PMID:016140324</ref><references group="xtra"/>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Ferrochelatase]]
[[Category: Ferrochelatase]]
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[[Category: Reimann, C T.]]
[[Category: Reimann, C T.]]
[[Category: Shipovskov, S.]]
[[Category: Shipovskov, S.]]
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[[Category: Lyase]]
[[Category: Pi-helix]]
[[Category: Pi-helix]]
[[Category: Rossman fold]]
[[Category: Rossman fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:33:00 2009''
 

Revision as of 10:13, 6 January 2013

Template:STRUCTURE 2ac2

Crystal structure of the Tyr13Phe mutant variant of Bacillus subtilis Ferrochelatase with Zn(2+) bound at the active site

Template:ABSTRACT PUBMED 16140324

About this Structure

2ac2 is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

  • Shipovskov S, Karlberg T, Fodje M, Hansson MD, Ferreira GC, Hansson M, Reimann CT, Al-Karadaghi S. Metallation of the transition-state inhibitor N-methyl mesoporphyrin by ferrochelatase: implications for the catalytic reaction mechanism. J Mol Biol. 2005 Oct 7;352(5):1081-90. PMID:16140324 doi:10.1016/j.jmb.2005.08.002

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