Dihydroxyacetone phosphate enamine intermediate in fructose-1,6-bisphosphate aldolase from rabbit muscle
The structure was published by St-Jean, M. and Sygusch, J., in 2007 in a paper entitled "Stereospecific proton transfer by a mobile catalyst in mammalian fructose-1,6-bisphosphate aldolase" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.88 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Fructose-bisphosphate aldolase A.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms homotetramers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: