phosphoglucose isomerase

Phosphoglucoisomerase

File 2PGI

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Rotate the molecule to display the binding pocket which is located between the two domains of this monomer protein.

Select arg202 or glu285 or lys139 or lys289 or lys420 or glu417 or tyr419
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These amino acids line the active site of the enzyme. The lys139 forms three salt bridges with the phosphate group on the glucose in order to stabilize the molecule. The lys420, glu417, and tyr419 form hydrogen bonds with the -OH groups on carbon #ís 3 and 4 of the G6P. A base catalyzed mechanism has been proposed for this reaction. This role is most likely carried out by glu285. To see this more clearly zoom in on the colored amino acid residues.

Primary Citation:
Sun, Y. J., Chou, C. C., Chen, W. S., Wu, R. T., Meng, M., Hsiao, C. D.: The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin.. Proc Natl Acad Sci U S A 96 pp. 5412 (1999)

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