1ado
From Proteopedia
(New page: 200px<br /><applet load="1ado" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ado, resolution 1.9Å" /> '''FRUCTOSE 1,6-BISPHOSP...) |
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| - | [[Image:1ado.gif|left|200px]]<br /><applet load="1ado" size=" | + | [[Image:1ado.gif|left|200px]]<br /><applet load="1ado" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ado, resolution 1.9Å" /> | caption="1ado, resolution 1.9Å" /> | ||
'''FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE'''<br /> | '''FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of fructose 1,6-bisphosphate aldolase shows three distinct | + | The structure of fructose 1,6-bisphosphate aldolase shows three distinct modes of product binding that are correlated to the disposition of the C-terminal region and depicts a possible trajectory for product exchange. The structure also indicates binding preference for monobasic triose phosphates. |
==About this Structure== | ==About this Structure== | ||
| - | 1ADO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with SO4 and 13P as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] Full crystallographic information is available from [http:// | + | 1ADO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=13P:'>13P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blom, N | + | [[Category: Blom, N S.]] |
[[Category: Sygusch, J.]] | [[Category: Sygusch, J.]] | ||
[[Category: 13P]] | [[Category: 13P]] | ||
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[[Category: schiff base]] | [[Category: schiff base]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:25 2008'' |
Revision as of 09:43, 21 February 2008
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FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE
Overview
The structure of fructose 1,6-bisphosphate aldolase shows three distinct modes of product binding that are correlated to the disposition of the C-terminal region and depicts a possible trajectory for product exchange. The structure also indicates binding preference for monobasic triose phosphates.
About this Structure
1ADO is a Single protein structure of sequence from Oryctolagus cuniculus with and as ligands. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Full crystallographic information is available from OCA.
Reference
Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase., Blom N, Sygusch J, Nat Struct Biol. 1997 Jan;4(1):36-9. PMID:8989320
Page seeded by OCA on Thu Feb 21 11:43:25 2008
