. 2005 Apr 28;24(10):1763–1774. doi: 10.1038/sj.emboj.7600663

Table 2. Dissociation constants (K_d) for nucleotide binding to PDK3 with and without L2.

Kinase	Nucleotide	K_d (μM)^a
PDK3	ADP	0.16±0.04 (n=3)
PDK3-L2	ADP	1.30±0.14 (n=3)
PDK3	ATP	0.16±0.005 (n=3)
PDK3-L2	ATP	0.84±0.10 (n=3)
PDK3	ATPγS	0.17
PDK3-L2	ATPγS	0.96
Dissociation constants for the binding of Mg-ADP, Mg-ATP, and Mg-ATPγS to MBP–PDK3 were measured by isothermal titration calorimetry in the absence and presence of lipoylated L2, as described in ‘Materials and methods'.
^aFor Mg-ADP and Mg-ATP in the absence or presence of L2, K_d values are expressed as mean±standard deviation. n=the number of experiments.

Table 2. Dissociation constants (Kd) for nucleotide binding to PDK3 with and without L2.