Previous proton and phosphorus nuclear magnetic resonance studies with yeast phosphoglycerate kinase have been extended using a higher-resolution spectrometer and a greater variety of binding agents. The new study shows that, apart from a few isolated mobile side chains distributed over the protein surface, there is a mobile section of phosphoglycerate kinase associated with the inter-domain region of the molecule. This region gives relatively well resolved resonances which are quite distinct from those originating from the remainder of the protein. This suggests that the molecule fluctuates between many states including several open or substrate binding forms in addition to the closed and supposedly catalytically competent form of the enzyme. The occupancy of these states appears to be affected by several anions including sulphate, phosphate and cobalticyanide, as well as substrates and their analogues.