Skip to main content
. Author manuscript; available in PMC: 2012 Mar 22.
Published in final edited form as: Biochemistry. 2011 Jan 26;50(11):1808ā€“1817. doi: 10.1021/bi101859k

Figure 4.

Figure 4

View of the isologous APAH dimer. (A) The L2 loop follows Ī²-strand 2; residues A81-I105 (colored green and yellow in their respective monomers) make extensive hydrophobic and hydrophilic interactions with the adjacent protomer that stabilize the APAH dimer. For reference, the active site Zn2+ ion is shown as a green sphere. (B) Small red spheres trace the ā€œLā€-shaped path from the dimer surface to the catalytic Zn2+ ion (green sphere).