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Figure 2 | BMC Microbiology

Figure 2

From: Discovery of novel inhibitors of Streptococcus pneumoniae based on the virtual screening with the homology-modeled structure of histidine kinase (VicK)

Figure 2

The modeled structure of the VicK HATPase_c domain of S. pneumoniae. (A) The solid ribbon representation of the structure model of the VicK HATPase_c domain. (B) Structure superposition of sketch of modeled VicK structure with the template. (C) Shape and surface features of the ATP-binding pocket of the VicK HATPase_c domain. The color denotes electrostatic potential of the protein surface. The red and blue color show negative and positive charged potential respectively, and the white surface means neutral potential of non-polar hydrophobic residues. The ATP-binding pocket is divided into "inner" and "outer" parts. The loop covered on the pocket is shown as tube for the sake of clearly demonstrating the hydrophobic inner part. The outer part of pocket is hydrophilic because of many polar residues in the entrance of the pocket, including the polar loop structure. All the pictures were generated by PyMol http://www.pymol.org/.

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BMC Microbiology

ISSN: 1471-2180

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