1.14.13.9	?	x * 50000, recombinant enzyme, SDS-PAGE	-, 676975	
1.14.13.9	?	x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE	-, 658919	
1.14.13.9	?	x * 60000, recombinant enzyme, SDS-PAGE	658918	
1.14.13.9	dimer	2 * 160000 in 0.2% Triton-X100, SDS-PAGE	348516	
1.14.13.9	homodimer	-	765266	
1.14.13.9	homodimer	ligand docking and human KMO model construction, overview	764520	
1.14.13.9	homodimer	the rat KMO monomer consists of three domains: alpha + beta flavin adenine dinucleotide (FAD)-binding domain I, FPMO enzyme-conserved domain II containing six-stranded beta-sheets, and C-terminal domain III, which is predicted to be comprising two transmembrane domains, although the exact topology remains ambiguous. The C-terminal region is comprising only one transmembrane domain, with the other predicted transmembrane helix lying laterally along the membrane, this helix displays hydrophobic residues on the outer side	764520	
1.14.13.9	additional information	structural analysis	658918	
1.14.13.9	additional information	the C-terminal region is required for the enzymatic activity and functions as a mitochondrial targeting signal	712322	
1.14.13.9	additional information	the structure of KMO can be realized as three domains: the first domain is where FAD is buried within beta-sheets and alpha-helices, one of which is the long alpha-helix that leads to the C-terminal domain. This helix and a loop that stands above the isoalloxazine rings of FAD define the borders of the active site in this region. The second region contains the residues of alpha-helices and beta-sheets whose side chains set the final border to the active site. Therefore, the active site is contained at the interface of the first and second regions. The third region of PfKMO consists of four alpha-helices while in scKMO and hKMO there are only the two alpha-helices of the transmembrane domain	765242