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Figure 4 | BMC Structural Biology

Figure 4

From: An unexpected phosphate binding site in Glyceraldehyde 3-Phosphate Dehydrogenase: Crystal structures of apo, holo and ternary complex of Cryptosporidium parvum enzyme

Figure 4

Comparison of the D-G3H binding sites in CpGAPDH, A and D subunit. A: Subunit A of CpGAPDH. Stick models are shown in white and red for subunit A; residues that bind to the C-3 phosphate and the active site residues (S153 and H180) are shown as sphere. The C3-phosphate occupies the 'new Pi site' in A, B and C subunits. B: Orientation of D-G3H molecule in subunit D of CpGAPDH (white and red stick) is different. There is no interaction between the phosphate oxygens and the phosphate binding loop.

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BMC Structural Biology

ISSN: 1472-6807

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