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3mk6

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[[Image:3mk6.jpg|left|200px]]
 
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{{STRUCTURE_3mk6| PDB=3mk6 | SCENE= }}
{{STRUCTURE_3mk6| PDB=3mk6 | SCENE= }}
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===Substrate and Inhibitor Binding to Pank===
===Substrate and Inhibitor Binding to Pank===
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{{ABSTRACT_PUBMED_20797618}}
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==Function==
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[[http://www.uniprot.org/uniprot/PANK3_HUMAN PANK3_HUMAN]] Plays a role in the physiological regulation of the intracellular CoA concentration (By similarity).
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{{ABSTRACT_PUBMED_20797618}}
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==About this Structure==
==About this Structure==
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3MK6 is a 4 chains structure with sequences 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=3MK6 OCA].
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[[3mk6]] is a 4 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=3MK6 OCA].
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==See Also==
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*[[Pantothenate kinase|Pantothenate kinase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:20797618</ref><references group="xtra"/>
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<ref group="xtra">PMID:020797618</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Pantothenate kinase]]
[[Category: Pantothenate kinase]]
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[[Category: Pank]]
[[Category: Pank]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 15 10:50:11 2010''
 

Revision as of 20:50, 17 April 2013

Template:STRUCTURE 3mk6

Contents

Substrate and Inhibitor Binding to Pank

Template:ABSTRACT PUBMED 20797618

Function

[PANK3_HUMAN] Plays a role in the physiological regulation of the intracellular CoA concentration (By similarity).

About this Structure

3mk6 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Leonardi R, Zhang YM, Yun MK, Zhou R, Zeng FY, Lin W, Cui J, Chen T, Rock CO, White SW, Jackowski S. Modulation of pantothenate kinase 3 activity by small molecules that interact with the substrate/allosteric regulatory domain. Chem Biol. 2010 Aug 27;17(8):892-902. PMID:20797618 doi:10.1016/j.chembiol.2010.06.006

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