1ado | pdb_00001ado

FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE

spinqualitylabelsall models 1ado, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ado is a 4 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 13P, SO4 Activity: Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ALDOA_RABIT] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aldolase 3D structures

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