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Figure 10 | BMC Structural Biology

Figure 10

From: Characterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics

Figure 10

Ribbon diagram of the crystal structure of FXa (PDB 2BOH) showing the identified interface regions. The figure highlights in red the regions corresponding to the identified interface residues from Fig. 9A and B. In the light chain: Arg86-Ser90 and Cys100-Asn105. In the heavy chain: Region I: Arg93; Phe101 (from the 99-loop). Region II: Arg125; Asp126; Glu129-Ser130; Thr134. Region III: Tyr162; Asp164-Asn166; Lys169; Leu170. Region IV: Gln178 and Asn179 (from the 174-loop). Region V: Lys230, Thr232, Ala233, Phe234 and Lys236 (residues from the C-terminal helix). Only residues present three or more times in the same column in the sequences are included. Light chain is in blue, heavy chain in purple. FXa is rotated 90° in a clockwise sense about its vertical axes with respect to Fig. 5. The terminal ends of FXa's chains are labeled. The catalytic triad is represented as cyan sticks.

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