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. 2013 Dec 12;8(12):e83181. doi: 10.1371/journal.pone.0083181

Table 2. Determination of sequential binding of ATP to PII-wt or PII-ST‑V variant.

Kd1 (µM) Kd2 (µM) Kd3 (µM)
PII-wt 4.8 ±0.0 17.4 ±1.5 92.8 ±14.1
PII-ST‑V 2.3 ±0.5 10.9 ±4.0 57.7 ±3.3

Mean values of three replicas of the calculated ATP dissociation constants for the PII binding sites 1-3 and ±SEM are shown. The original isotherms are presented in Figure S2.