Data on molecular docking of tautomers and enantiomers of ATTAF-1 and ATTAF-2 selectivty to the human/fungal lanosterol-14α-demethylase

The data have been obtained for tautomers and enantiomers of ATTAF-1 and ATTAF-2 that were developed based on antifungal standard drugs with triazole scaffold. These compounds were docked into the human and fungal lanosterol-14α-demethylase. In order to validate the data, 8 standard triazole antifungal drugs (Fluconazole, Itraconazole, Posaconazole, Ravuconazole, Albaconazole, Voriconazole, Isavuconazole and Efinaconazole) were also docked into the human and fungal lanosterol-14α-demethylase. The binding conformations of these molecules and their interactions with lanosterol-14α-demethylase may inform the development of further small molecule lanosterol-14α-demethylase inhibitors with significant selectivity toward this enzyme. The analysis has done on the basis of type of interactions (bond type and distance). The length of the Fe-N coordination bond for (R)-N2-ATTAF-1 and (S)-N1-ATTAF-2 complexes is obtained 6.36 and 4.19 Å, respectively and about 2 Å in the other tautomer and enantiomer complexes, reflecting the lower basicity of the N-4 atom in the 1,2,4-triazole ring of (R)-N2-ATTAF-1 and (S)-N1-ATTAF-2 in comparison with the N-4 atom in the 1,2,4-triazole ring in other tautomers and enantiomers and supporting higher selectivity of (R)-N2-ATTAF-1 and (S)-N1-ATTAF-2 towards the target CYP51 enzymes vs. human. Interestingly, we have investigated unfavorable interactions (donor-donor) with TRP239 and MET378 for (R)-N2-ATTAF-1 and (S)-N1-ATTAF-2, respectively. These unfavorable interactions also have been seen in case of posaconazole and isavuconazole. The data presented in this article are related to the research paper entitled "In silico prediction of ATTAF-1 and ATTAF-2 selectivity towards human/fungal lanosterol 14α-demethylase using molecular dynamic simulation and docking approaches".


Value of the data
• The lanosterol 14 α-demethylase has been identified as a molecular target for the treatment of fungal diseases.
• The modeling data was produced to rationalize the structural necessities for lanosterol 14 αdemethylase inhibition. • The binding conformations of the ATTAF-1 and ATTAF-2, their interactions with human and fungal lanosterol 14 α-demethylase and coordination bond distance may inform further studies focused on the development of lanosterol 14 α-demethylase inhibitors.
• Novel synthetic analogues with improved bioactivity and minimized side effects can be expanded against this target by using this in silico docking data and research time can be minimized significantly. • This dataset can be useful to model other potent antifungal agents in future and researchers in pharmaceutical chemistry can gain from the data.

Data description
Lanosterol-14 α-demethylase (CYP51) is found in mycobacteria, fungi, plants, animals and humans. This enzyme is required for biosynthesis of sterol in eukaryotes and is the major target for azole antifungal agents [ 1 , 2 ]. In mammals, lanosterol-14 α-demethylase is the enzyme that catalyzes lanosterol to cholesterol conversion, which is necessary to maintain a variety of metabolic functions [3] . An ideal antifungal agent should have minimal effect on human CYP51 enzymes while keeping potent inhibition of fungal enzyme to reduce the side effects [4] . Lanosterol-14 α-demethylase consists of an iron protoporphyrin unit in its active site. At the molecular level, N-4 in the 1,2,4-triazole ring selectively coordinates to the lanosterol-14 α-demethylase heme iron and cause the prevention of the fungal ergosterol biosynthesis pathway [5] . In order support a medicinal chemistry campaign to develop potent azole antifungal agents with high CYP51 affinity, we have previously synthesized and reported a series of novel fluconazole analogues, with the most promising ones introduced as ATTAF-1 and ATTAF-2 [6] and provided the computational-based docking and MD simulation outputs for all tautomeric and enantiomeric forms of ATTAF-1 and ATTAF-2 plus 8 antifungal standard drugs were docked into the human and fungal lanosterol-14 α-demethylase [9] . Here, our studies provide important protein-ligand interaction information for the further development of lanosterol-14 α-demethylase inhibitors. In this article Table 1 provides the details about the targets and their description. Table 2 gives the coordinates of the cubic box used to dock ATTAF-1 and ATTAF-2 to the fungal and human CYP51. Table 3 gives the length of the Fe-N coordination bond. Table 4

Protein selection and preparation
The crystal structures of the selected proteins were retrieved from protein data bank. (PDB database, www.rcsb.org ). Protein preparation was done by preprocessing the structures by re-      moving water molecules, ions and cocrystallized ligands, polar hydrogens addition and assigning Gasteiger-Marsili partial charges, adjusting bonds and formal charges for metals, and removing unwanted chains. In order to rmsd validation, the co-crystallized ligand was re-docked. The target input files were converted to PDBQT format for AutoDock by using the AutoDockTools-1. 5. 4.

Ligand preparation and molecular docking
Ligands 3D structures were sketched by using ChemDraw Ultra 8.0 and energy minimized using PM3 force field. For all ligands, the nonpolar hydrogen atoms were merged and the Gasteiger charges were assigned. Then set number of torsion with detect root and choose torsion in Autodock program. Later, ligand input files were also saved as PDBQT format utilizing the AutoDock Tools. The minimized structures were docked on the prepared protein.
Discovery Studio Client 2016 and Molegro Molecular Viewer were used for further analysis.

Declaration of Competing Interest
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Supplementary materials
Supplementary material associated with this article can be found, in the online version, at doi: 10.1016/j.dib.2020.105942 .