Capturing dynamic aspects of proteins in solution is not always straightforward, especially for multi domain proteins. This study exploits paramagnetic lanthanide probes in NMR and EPR to visualize conformational states and ligand-induced conformational changes of a multidomain protein enzyme MurD, consisting of three domains. The previous crystallographic study identified that MurD takes at least two conformations, open and closed conformations, in which the conformation of domain 3 varies significantly. However, details about the conformational states and changes coupled with the enzymatic process remained unclear. To study conformational states of MurD in solution, paramagnetic lanthanide ions were attached to the domain 2 for NMR study and to the domain 2 and 3 for EPR study. NMR study using pseudo-contact shift identified a novel conformational state of MurD named “semi-closed state”. EPR measurement of inter-lanthanide distance revealed that MurD in the absence of the ligand exists in a wide variety of conformational states that was eliminated upon binding to the ligand. The data highlighted that conformational flexibility of MurD in solution that was corroborated by NMR dynamics study and molecular dynamics simulation. In this presentation, the functional importance of the conformational states and dynamics of MurD will be discussed.