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. 2004 Jul 27;381(Pt 3):561–579. doi: 10.1042/BJ20040752

Figure 5. 3D structure of one enzyme subunit of the testis PFK-2/FBPase-2 isoenzyme.

Figure 5

The co-ordinates were retrieved from the PDB database (accession code 1BIF) containing ATPγS in the PFK-2 domain. The position of Fru-6-P was modelled as described in [44]. In the upper right hand PFK-2 domain, ATP is on the left and Fru-6-P is on the right. In the lower left hand FBPase-2 domain, two inorganic phosphates indicate the position of the Fru-2,6-P2-binding site. The PFK-2 domain is composed of a β-sheet surrounded by α-helices. Two subdomains, composed of α-helices (above) form a flexible cover and are involved in Fru-6-P binding and catalysis (induced fit, see text).