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. Author manuscript; available in PMC: 2009 Oct 14.
Published in final edited form as: Biochemistry. 2008 Sep 20;47(41):10933–10939. doi: 10.1021/bi8008278

Figure 2.

Figure 2

A) Schematic drawing of TMEGF45 showing the residues identified as important for the cofactor activity of TM. Residues are colored according to location: fourth domain in green, linker region in purple, Met388 in cyan, and fifth domain in red. B) Crystal structure of the thrombin-TMEGF456 complex. The important TM residues are shown as sticks and colored as in A. ABE1 of thrombin is blue and shown in sticks. The active site catalytic triad of thrombin is shown as green sticks.