Modelación por homología de la proteína Luxs de Porphyromonas gingivalis cepa W83

background: crystallization is not always achieved for all proteins in a good size and a good quality for x-ray diffraction. so that condition opens a field for the development of theoretical molecular and protein studies allowing the representation of the molecules in 3d, providing spatial information to study the interaction between ligands and macromolecular receptors. materials and methods: in silico study from primary sequence analysis of six different proteins luxs crystallized of several bacteria. 1j6x protein of helicobacter pylori was selected for its similarity with the luxs protein sequence in porphyromonas gingivalis (p. gingivalis) strain w83 to produce a homology model of this protein, using the sybyl and moe software. a docking was performed to assess the reproducibility of the model in a biological environment. results: the luxs protein modelling of p. gingivalis strain w83 was developed, which allows the approach to a proposed structure for the interaction between the protein and its natural ligand. the model generated with computational resources achieved the correct position and biological behavior by means of developed calculations. the docking showed a cavity in which the ligand adopted several positions with good results. conclusions: a luxs protein model was obtained, validated by different methods. this generated a 3d model for luxs protein in p. gingivalis strain w83 with biological reproducibility by means of molecular docking.