Fig 1.
A brief overview of the research methodology.
Table 1.
Subtractive filtering of proteins from Gardenerella vaginalis in the current investigation.
Fig 2.
(A) A diagram displaying the shortlisted proteins’ subcellular localization (B) A protein-protein interaction diagram utilizing the STRING database.
Table 2.
List of STRING interactions shown in tabular format.
Fig 3.
(A) modeled structure of phospho-2-dehydro-3-deoxyheptonate aldolase and (B) shows the 4HSO Template protein (green color) superimposed on the modeled protein structure (blue color) Having the percent identity of 88% (C) the PROCHEK validation of modeled structure, and (D) The Prosa web score (z = -9.11) for the phospho-2-dehydro-3-deoxyheptonate aldolase structure.
Fig 4.
Redocking of a co-crystallized phospho-2-dehydro-3-deoxyheptonate aldolase ligand (cysteine) within the phospho-2-dehydro-3-deoxyheptonate aldolase active site, displaying an RMSD of 1.9Å.
Fig 5.
Virtual screening results of the 9213 FDA approved drugs against phospho-2-dehydro-3-deoxyheptonate aldolase (A) The virtual screening results of the protein against the FDA Approved library showed that the binding affinities ranged from -6.9 to 0.3 kcal/mol. (B) selecting a small number of these chemicals to be used in the current investigation.
Fig 6.
A molecular docking analysis of the molecules DB03332, DB07452, DB01262, DB02076 and DB00727 demonstrating the 2D interaction of ligands produced using Discovery studio shown as (A), (B), (C), (D) and (E), respectively.
Table 3.
The shortlisted five compounds’ ADME profiles measured against phospho-2-dehydro-3-deoxyheptonate aldolase.
Table 4.
The toxicity profiling for shortlisted five compounds against the phospho-2-dehydro-3-deoxyheptonate aldolase protein.