Aim: Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme which plays a key role in
fatty acid biosynthesis via production of melonyl-CoA as an essential substrate. It is
involved in homeostasis of fatty acids inside the system using both up and down regulating
mechanisms. Apart from this In silico analysis of its catalytic site and regulatory sites make
it a potential target for herbicidal and insecticidal drug targeting. Currently the 3D structure
of Acetyl-CoA carboxylase (ACC) from Jatropha curcas has not been solved in Protein
Data Bank (PDB). Hence the aim of the present study is to build the 3D structure of AcetylCoA
carboxylase (ACC) from J. curcas also to perform a virtual screening for the identifi-
cation of the effective inhibitors using molecular docking studies.
Methods: Homology modeling has been used to determine the 3D structure of Acetyl-CoA
carboxylase (ACC) from J. curcas. Structure validation and molecular docking studies has
been carried out using Procheck and Molegro Virtual Docker respectively.
Results: Ramachandran Plot confirmed quality of modeled structures along with main chain
and side chain parameters. Out of 309 residues in SPDBV model, 244 were in core region 19
residues were in additional allowed region, 2 residues were in generous allowed region and
no residues were in disallowed region.
Conclusion: Energy minimization for SPDBV model thermodynamically proved accepted
structure with energy of 12,063.024 kJ/mol. The model further can be subjected to pharmacodynamic
and pharmacokinetic studies. Molecular docking studies identified few
established herbicides which could be promising inhibitors of Acetyl-CoA carboxylase
(ACC). Efforts to screen and identify ACC inhibitors using flexible molecular docking
resulted in Pinoxaden from Phenylpyrazole class as the most effective inhibitor with
rerank ¼ 81.436 and RMSD ¼ 0.31.