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1ADO

FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE

Summary for 1ADO
Entry DOI10.2210/pdb1ado/pdb
DescriptorALDOLASE, 1,3-DIHYDROXYACETONEPHOSPHATE, SULFATE ION, ... (4 entities in total)
Functional Keywordsaldolase, lyase (aldehyde), schiff base, glycolysis, lyase
Biological sourceOryctolagus cuniculus (rabbit)
Total number of polymer chains4
Total formula weight157546.79
Authors
Blom, N.S.,Sygusch, J. (deposition date: 1996-12-02, release date: 1997-12-24, Last modification date: 2024-04-03)
Primary citationBlom, N.,Sygusch, J.
Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase.
Nat.Struct.Biol., 4:36-39, 1997
Cited by
PubMed Abstract: 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.
PubMed: 8989320
DOI: 10.1038/nsb0197-36
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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