Skip to main content
. Author manuscript; available in PMC: 2013 Jan 20.
Published in final edited form as: Biochemistry. 2011 Nov 8;50(47):10195–10202. doi: 10.1021/bi2015019

Figure 2. Active site accessibility in prethrombin-2.

Figure 2

The collapsed form of prethrombin-2 (orange) features a cluster of hydrophobic/aromatic residues that completely occludes access to the active site, as observed in the recent structure of prethrombin-1 (17). The cluster is formed by the collapse of W215 and W148 into the active site against W60d, with the indole ring of W215 moving >10 Å relative to its position in the open form (yellow). The electron density 2F0-Fc map (green mesh) outlines the alternative positions of W215 and is contoured at 1 σ.