Skip to main content
. Author manuscript; available in PMC: 2011 Aug 10.
Published in final edited form as: Biochemistry. 2010 Aug 10;49(31):6737–6745. doi: 10.1021/bi100912m

FIGURE 2.

FIGURE 2

Overall chain fold of dimeric human sfALR. The two C95-C204 disulfides that join the gray and green subunits of the sfALR homodimer are shown in yellow, together with the redox-active proximal disulfide (C142–C145) and the structural disulfide (C171–C188) in the gray subunit. The FAD is depicted in yellow.