Aldehyde dehydrogenase monomer complexed with NAD (Animation)

Science: J. Hempel, J. Perozich and H.B. Nicholas Jr (A) University of Pittsburgh and (A) PSC; Animation: David W. Deerfield II, PSC.
The highly conserved residues are in magenta while the remaining residues are in cyan. The NAD is in green. The animation starts with the the protein in a CPK representation, followed by a bond representation (with the NAD still in CPK) and then a spline through the backbone positions. The NAD fades from a CPK to bond representation and then fades out. The animation finished with the spline representation playing tumble weed.

ADDITIONAL ANIMATIONS OF ALDH:

CPK representation of ALDH. Start with dimer from the "backside" followed by a half rotation and then zoom into one of the active sites. The blue residue (Asp247) in the upper middle of the final image and the GREEN residues (100% conserved) are discussed in:
Hempel, J., Kuo, I., Perozich, J., Wang, B-C., Lindahl, R., and Nicholas, H. 2001. Aldehyde dehydrogenase: Maintaining critical active site geometry at motif 8 in the class 3 enzyme. European Journal of Biochemistry Vol. 268. pp. 722-726. (5.5 MB)

SPLINE representation of ALDH. Starts with a closeup of one of the active sites with the appropriate side chains represented as "bonds" or as a single sphere (for the C(alpha) of glycine). The animation then rotates up and then down giving one a clear idea of the packing around the active site. (1.5M)

Small SPLINE of entire dimer (157K)
Small SPLINE of NAD site. (157K)