We performed a coarse-grained simulation of Pseudomonas Aeruginosa azurin using the implementation of G<overline>o</overline> model. We probe the unfolding dynamics of oxidized structure of copper-containing H117G (Cu-H117G) azurin. In vitro, the kinetic experiments have shown that both of the wild type and H117G azurins fold in apparent two-state reactions. Here we analyze the transition state of azurin based on energy landscape theory. The transition state which is indicated by free energy barrier between the denatured state and native state has been found on the simulation near the folding temperature. We simulated for several fixed temperature and found that mutated azurin unfolds faster than wild-type azurin. Moreover, we also calculated the φ-value which is widely used in experimental studies for reconstructing protein-folding transition state and is most powerful when in combination with simulation. By this analysis, we determine which region of azurin folds faster than others and compare the results with experimental data.