Skip to main content
. Author manuscript; available in PMC: 2014 Oct 1.
Published in final edited form as: Medchemcomm. 2013 Oct;4(10):10.1039/C3MD00219E. doi: 10.1039/C3MD00219E

Fig. 2.

Fig. 2

(A) Alignment of NVPro and HOVPro protein sequence. The conserved residues that compose the S2 pockets of the two proteins are labeled with a bracket and a major difference is highlighted red letters; (B) Superposition of the crystal structure of NVPro (PDB: 2FYQ) shown in cyan and a homology model of HOVPro structure in gold. The S2 pocket loop (bII-cII) shows a different conformation in the HOV protease, which appears to be due to the Gly115 residue. In the NV protease the residue at the 115 position is His; (C) Tables depict the conserved residues that compose the S1, S2 and S4 pockets, in NV and HOV proteases.