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PDBe Entry: 2quu 
Dihydroxyacetone phosphate Schiff base intermediate in mutant fructose-1,6-bisphosphate aldolase from rabbit muscle
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LYASE
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X-RAY DIFFRACTION
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Resolution: 1.98 Å, R-factor: 15.7%, Free R-factor: 19.5%, Spacegroup: P 1 21 1
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28/08/2007, deposition: 06/08/2007, last revision: 24/02/2009
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St-Jean, M. ; Sygusch, J.
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Stereospecific proton transfer by a mobile catalyst in mammalian fructose-1,6-bisphosphate aldolase J.BIOL.CHEM. vol:282, pag:31028-31037 (2007) [PubMed ID 17728250 ]
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aldolase , mutant , substrate , Schiff base , protonated imine , intermediate , covalent , Acetylation , Glycolysis , Lyase , Phosphorylation
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4.1.2.13 ExPASy BRENDA (A B C D)
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Oryctolagus cuniculus(rabbit) 9986 (A B C D)
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Fructose-bisphosphate aldolase A (EC 4.1.2.13) (Muscle-type aldolase) P00883 (A B C D)
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A, B, C, D
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1zah, 2qut, 2quv
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| A, B, C, D |
Fructose-bisphosphate aldolase A |
Protein |
P00883 (ALDOA_RABIT)
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363 |
100% |
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| A, B, C, D |
1,3-DIHYDROXYACETONEPHOSPHATE |
13P
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