L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T
The structure was published by Dreyer, M.K. and Schulz, G.E., in 1996 in a paper entitled "Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.92 Å and deposited in 1996.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of L-FUCULOSE-1-PHOSPHATE ALDOLASE. This molecule has the UniProt identifier P0AB87 (FUCA_ECOLI). The sample contained 215 residues which is 100% of the natural sequence. Out of 215 residues 206 were observed and are deposited in the PDB.
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: