2.5.1.46	at 2.2 A a new form II crystal of the deoxyhypusine synthase:NAD holoenzyme is grown at low ionic strength and pH 8.0, near the optimal pH for enzymatic activity	659357	
2.5.1.46	heterotetramer, to 3.5 A resolution. The activity is dependent on heterotetramer formation between paralogs DHSc and DHSp. The X-ray structure of DHS shows a single functional shared active site formed at the DHSc/DHSp heterodimer interface. Deficiencies in one subunit are complemented by the other	760209	
2.5.1.46	in complex with inhibitors 6-bromo-N-(1H-indol-4-yl)-1-benzothiophene-2-carboxamide and N''-guanyl-1,7-diaminoheptane. Presence of 6-bromo-N-(1H-indol-4-yl)-1-benzothiophene-2-carboxamide induces a dramatic conformational change in DHPS	759614	
2.5.1.46	structures of the apoprotein, as well as ligand-bound states at 1.41 to 1.69 A resolution. Polyamines namely spermine and putrescine bind DHS in a similar manner as spermidine. Spermine may to some extent serve as an alternative DHS substrate. No conformational changes occur in the DHS structure upon spermidine binding. A conserved ball-and-chain motif is indispensable to assembling a functional DHS tetramer	758884	
2.5.1.46	vapor diffusion in hanging drops, crystal structure of the enzyme-NAD complex at 2.2 A resolution	638071