2yce
From Proteopedia
(Difference between revisions)
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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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- | (as it appears on PubMed at http://www.pubmed.gov), where 15766250 is the PubMed ID number. | ||
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{{ABSTRACT_PUBMED_15766250}} | {{ABSTRACT_PUBMED_15766250}} | ||
==About this Structure== | ==About this Structure== | ||
- | [[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]. | + | [[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== | ||
+ | *[[Aldolase|Aldolase]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <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.]] | ||
+ | [[Category: Glycolysis]] | ||
+ | [[Category: Lyase]] |
Revision as of 10:31, 26 July 2012
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