1ADO
FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE
Summary for 1ADO
Entry DOI | 10.2210/pdb1ado/pdb |
Descriptor | ALDOLASE, 1,3-DIHYDROXYACETONEPHOSPHATE, SULFATE ION, ... (4 entities in total) |
Functional Keywords | aldolase, lyase (aldehyde), schiff base, glycolysis, lyase |
Biological source | Oryctolagus cuniculus (rabbit) |
Total number of polymer chains | 4 |
Total formula weight | 157546.79 |
Authors | Blom, N.S.,Sygusch, J. (deposition date: 1996-12-02, release date: 1997-12-24, Last modification date: 2024-04-03) |
Primary citation | Blom, 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: 8989320DOI: 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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