1ado

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{{STRUCTURE_1ado| PDB=1ado | SCENE= }}
{{STRUCTURE_1ado| PDB=1ado | SCENE= }}
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'''FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE'''
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===FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8989320 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8989320}}
==About this Structure==
==About this Structure==
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[[Category: Glycolysis]]
[[Category: Glycolysis]]
[[Category: Schiff base]]
[[Category: Schiff base]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:08:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:38:09 2008''

Revision as of 13:38, 30 June 2008

Image:1ado.png

Template:STRUCTURE 1ado

FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE

Template:ABSTRACT PUBMED 8989320

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 Mon Jun 30 16:38:09 2008

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