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1ado

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|PDB= 1ado |SIZE=350|CAPTION= <scene name='initialview01'>1ado</scene>, resolution 1.9&Aring;
|PDB= 1ado |SIZE=350|CAPTION= <scene name='initialview01'>1ado</scene>, resolution 1.9&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>
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|LIGAND= <scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ado FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ado OCA], [http://www.ebi.ac.uk/pdbsum/1ado PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ado RCSB]</span>
}}
}}
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[[Category: Blom, N S.]]
[[Category: Blom, N S.]]
[[Category: Sygusch, J.]]
[[Category: Sygusch, J.]]
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[[Category: 13P]]
 
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[[Category: SO4]]
 
[[Category: aldolase]]
[[Category: aldolase]]
[[Category: glycolysis]]
[[Category: glycolysis]]
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[[Category: schiff base]]
[[Category: schiff base]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:56:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:38:03 2008''

Revision as of 15:38, 30 March 2008


PDB ID 1ado

Drag the structure with the mouse to rotate
, resolution 1.9Å
Ligands: ,
Activity: Fructose-bisphosphate aldolase, with EC number 4.1.2.13
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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