Table 2.

Thermodynamics for binding adenine and transition state analogue inhibitors to human MTAP.

Inhibitor	Kd [n]a (nM)	ΔG (kcal/mol)	ΔH (kcal/mol)	−TΔS (kcal/mol)
Adenine	3000 ± 1000b [1]	−7.6 ± 0.2	−0.003 ± 0.2	−7.6 ± 0.3
	2100 ± 80b [1]	−7.7 ± 0.2	2.4 ± 0.2	−10.1 ± 0.3
	80000 ± 80000b [1]	−5.6 ± 0.5	−2.6 ± 0.8	−3.0 ± 0.9
MT-ImmA	1.0 ± 0.1c [2.42 ± 0.04]	−12.3 ± 0.1	0.24 ± 0.04	−12.5 ± 0.1
	700 ± 300b [0.58 ± 0.09]	−8.4 ± 0.3	2.7 ± 0.4	−11.1 ± 0.5
nPrT-ImmA	0.214 ± 0.01c [2.13 ± 0.04]	−13.2 ± 0.03	0.24 ± 0.03	−13.4 ± 0.1
	900 ± 600b [0.9 ± 0.1]	−8.2 ± 0.4	1.1 ± 0.2	−9.3 ± 0.4
MT-DADMe-ImmA	0.09 ± 0.01d [3]	−13.7 ± 0.1	1.5 ± 0.1	−15.2 ± 0.1
EtT-DADMe-ImmA	0.034 ± 0.003d [3]	−14.3 ± 0.1	1.8 ± 0.1	−16.1 ± 0.1
p-Cl-PhT-DADMe-ImmA	0.010 ± 0.005d [3]	−15.0 ± 0.3	2.6 ± 0.1	−17.6 ± 0.3

^an is the number of sites.

^bK_d values are derived from ITC data fitting.

^cFrom reference (9).

^dFrom reference (5).