Abstract
The three-dimensional structure of phosphoglycerate mutase has been analyzed using a contoured distance matrix and by visual inspection using three-dimensional computer graphics. Three folding lobes have been identified and their internal structure tentatively characterized. The active site is located at a lobe interface with a channel providing possible access from above and below. The arrangement of active site residues on two lobes suggests that the active site might be conformationally flexible. The remaining interface not associated with the active site channel appears to be predominately hydrophobic and thus may contribute to inter-lobe stability.
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