Figure 2From: An unexpected phosphate binding site in Glyceraldehyde 3-Phosphate Dehydrogenase: Crystal structures of apo, holo and ternary complex of Cryptosporidium parvum enzymeCofactor induced conformational changes in active site histidine (H180). A: Movement of the active site histidine residue in subunits A and D. Apo (white), Holo (yellow); B: In subunits B and C H180 remains in the same position in the apo and holo forms.Back to article page