2ac2
From Proteopedia
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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== | ||
- | + | [[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== | ||
- | <ref group="xtra">PMID: | + | <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.]] | ||
+ | [[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
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