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. Author manuscript; available in PMC: 2018 Oct 1.
Published in final edited form as: J Thromb Haemost. 2017 Sep 1;15(10):2005–2016. doi: 10.1111/jth.13788

Figure 8.

Figure 8

Comparison of phosphate binding site for A) prothrombin-GLA co-crystallized with a single lysoPS (PDB 1NL2) [8], and B) FX-GLA bound to PS from one of our full-membrane simulations. Binding of PS is similar in both cases, with the equivalent starboard face residues (ARG10 and ARG16 on prothrombin-GLA, LYS9 and ARG15 on FX-GLA) interacting with the phosphate group. SER3 in FX-GLA does not interact with the phosphate, however, unlike LYS3 in the prothrombin structure.