Figure 3.
Fig. 3. A, a section through the C trace of
the apoenzyme subunit showing the large internal solvent-filled
cavity. For clarity, the FAD cofactor and
4-(trifluoromethyl)phenol as bound in the holo H61T ternary
complex were superimposed and shown in yellow and blue,
respectively. The surface was calculated using MSMS (28) and the
picture was generated using DINO (27). B, superposition of
active site residues in the apo (green) and the holo form
complexed with 4-(trifluoromethyl)phenol (red) structures of the
VAO H61T mutant. The figure was prepared with MOLSCRIPT ( 26).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2000,
275,
38654-38658)
copyright 2000.
trace of
the apoenzyme subunit showing the large internal solvent-filled
cavity. For clarity, the FAD cofactor and
4-(trifluoromethyl)phenol as bound in the holo H61T ternary
complex were superimposed and shown in yellow and blue,
respectively. The surface was calculated using MSMS (28) and the
picture was generated using DINO (27). B, superposition of
active site residues in the apo (green) and the holo form
complexed with 4-(trifluoromethyl)phenol (red) structures of the
VAO H61T mutant. The figure was prepared with MOLSCRIPT ( 26).