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4aop

From Proteopedia

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==About this Structure==
==About this Structure==
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4AOP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AOP OCA].
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4AOP is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AOP OCA].
==Reference==
==Reference==
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Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange., Crane BR, Siegel LM, Getzoff ED, Biochemistry. 1997 Oct 7;36(40):12101-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9315848 9315848]
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<ref group="xtra">PMID:9315848</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
 
[[Category: Crane, B R.]]
[[Category: Crane, B R.]]
[[Category: Getzoff, E D.]]
[[Category: Getzoff, E D.]]
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[[Category: Siroheme feii]]
[[Category: Siroheme feii]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:28:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:01:49 2009''

Revision as of 22:01, 17 February 2009

Template:STRUCTURE 4aop

SULFITE REDUCTASE HEMOPROTEIN PARTIALLY PHOTOREDUCED WITH PROFLAVINE EDTA, PHOSPHATE PARTIALLY BOUND

Template:ABSTRACT PUBMED 9315848

About this Structure

4AOP is a 1 chain structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Crane BR, Siegel LM, Getzoff ED. Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange. Biochemistry. 1997 Oct 7;36(40):12101-19. PMID:9315848 doi:10.1021/bi971065q

Page seeded by OCA on Wed Feb 18 00:01:49 2009

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