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2yce

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[[Image:2yce.jpg|left|200px]]
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{{STRUCTURE_2yce| PDB=2yce | SCENE= }}
{{STRUCTURE_2yce| PDB=2yce | SCENE= }}
===STRUCTURE OF AN ARCHAEAL FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE WITH THE CATALYTIC LYS COVALENTLY BOUND TO THE CARBINOLAMINE INTERMEDIATE OF THE SUBSTRATE.===
===STRUCTURE OF AN ARCHAEAL FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE WITH THE CATALYTIC LYS COVALENTLY BOUND TO THE CARBINOLAMINE INTERMEDIATE OF THE SUBSTRATE.===
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{{ABSTRACT_PUBMED_15766250}}
{{ABSTRACT_PUBMED_15766250}}
==About this Structure==
==About this Structure==
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[[2yce]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1w8r 1w8r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YCE OCA].
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[[2yce]] is a 10 chain structure of [[Aldolase]] with sequence from [http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1w8r 1w8r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YCE OCA].
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==See Also==
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*[[Aldolase|Aldolase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:15766250</ref><references group="xtra"/>
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<ref group="xtra">PMID:015766250</ref><references group="xtra"/>
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Thermoproteus tenax]]
[[Category: Thermoproteus tenax]]
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[[Category: Pohl, E.]]
[[Category: Pohl, E.]]
[[Category: Siebers, B.]]
[[Category: Siebers, B.]]
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[[Category: Glycolysis]]
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[[Category: Lyase]]

Revision as of 10:31, 26 July 2012

Template:STRUCTURE 2yce

Contents

STRUCTURE OF AN ARCHAEAL FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE WITH THE CATALYTIC LYS COVALENTLY BOUND TO THE CARBINOLAMINE INTERMEDIATE OF THE SUBSTRATE.

Template:ABSTRACT PUBMED 15766250

About this Structure

2yce is a 10 chain structure of Aldolase with sequence from Thermoproteus tenax. This structure supersedes the now removed PDB entry 1w8r. Full crystallographic information is available from OCA.

See Also

Reference

  • Lorentzen E, Siebers B, Hensel R, Pohl E. Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates. Biochemistry. 2005 Mar 22;44(11):4222-9. PMID:15766250 doi:http://dx.doi.org/10.1021/bi048192o

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