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2heg

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[[Image:2heg.png|left|200px]]
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{{STRUCTURE_2heg| PDB=2heg | SCENE= }}
{{STRUCTURE_2heg| PDB=2heg | SCENE= }}
===Phospho-Aspartyl Intermediate Analogue of Apha class B acid phosphatase/phosphotransferase===
===Phospho-Aspartyl Intermediate Analogue of Apha class B acid phosphatase/phosphotransferase===
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{{ABSTRACT_PUBMED_018845157}}
==About this Structure==
==About this Structure==
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2HEG is a 2 chains structure of sequences 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=2HEG OCA].
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[[2heg]] is a 2 chain structure of [[Acid phosphatase]] with 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=2HEG OCA].
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==See Also==
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*[[Acid phosphatase|Acid phosphatase]]
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==Reference==
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<ref group="xtra">PMID:018845157</ref><references group="xtra"/>
[[Category: Acid phosphatase]]
[[Category: Acid phosphatase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Apha class b acid phosphatase/phosphotransferase]]
[[Category: Apha class b acid phosphatase/phosphotransferase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 02:20:51 2009''
 

Revision as of 04:39, 26 July 2012

Template:STRUCTURE 2heg

Contents

Phospho-Aspartyl Intermediate Analogue of Apha class B acid phosphatase/phosphotransferase

Template:ABSTRACT PUBMED 018845157

About this Structure

2heg is a 2 chain structure of Acid phosphatase with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

Reference

  • Leone R, Cappelletti E, Benvenuti M, Lentini G, Thaller MC, Mangani S. Structural insights into the catalytic mechanism of the bacterial class B phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases. J Mol Biol. 2008 Dec 12;384(2):478-88. Epub 2008 Sep 27. PMID:18845157 doi:10.1016/j.jmb.2008.09.050

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