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-14 alpha-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-14 alpha-demethylase. The bind ing conformations of these molecules and their interactions with lanosterol-14 alpha-demethylase may inform the development of further small molecule lanosterol-14 alpha-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 angstrom, respectively and about 2 angstrom 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 14 alpha-demethylase using molecular dynamic simulation and docking approaches". (c) 2020 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license. (http://creativecommons.org/licenses/by/4.0/ )
