1ado: Difference between revisions
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|PDB= 1ado |SIZE=350|CAPTION= <scene name='initialview01'>1ado</scene>, resolution 1.9Å | |PDB= 1ado |SIZE=350|CAPTION= <scene name='initialview01'>1ado</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|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] | |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= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|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.]] | ||
[[Category: aldolase]] | [[Category: aldolase]] | ||
[[Category: glycolysis]] | [[Category: glycolysis]] | ||
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[[Category: schiff base]] | [[Category: schiff base]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''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
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| 1ado, resolution 1.9Å | |||||||||||||
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| Ligands: | 13P, SO4 | ||||||||||||
| 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
Page seeded by OCA on Sun Mar 30 18:38:03 2008
