Galaxy is an international bioinformatics platform for biologists [1] . So far, the Galaxy team has adapted molecular dynamics tools which are mainly tools to create the prerequisites of a simulation or to run a simulation. In our case, this simulation step was done but the tools to finalize our analysis were missing. This is why tools have been developed and integrated in Galaxy. This integration of a succession of internal tools in the form of a Galaxy workflow is intended to help biologists and would benefit from the high performance computing facilities connected to the Galaxy webservice. Tools developed here aim at studying the structure the structure of 102 aquaporin trajectories using a molecular dynamics approach. This approach requires to take into account the molecular scale (Ångströms) of the proteins and the time step (nanosecond). In total, we speak of a simulated trajectory of 100 ns to model the transport of a water molecule [2]. In order to optimize the computational time on a trajectory, each trajectory is divided into several sub-trajectories and the pore diameter calculations are performed for each sub-trajectory. The resulting data are then compiled in a table before being visualized in graphical form. This workflow is designed to work on aquaporin trajectories. Aquaporins are transmembrane proteins that transport water. In addition, an aquaporin is a tetramer composed of four protomers. Each protomer has six transmembrane alpha helices connected by extramembrane loops that structure into a central pore. In addition, each protomer is hourglass-shaped and has two sites consisting of 3 successive amino acids, Asparagine - Proline - Alanine (NPA) and an aromatic arginine site (arR) [3]. The NPA sites form an electro-static barrier preventing excess protons from entering the cell. The arR site is composed of 4 amino acids that form a constriction inside the pore of each protomer. This constriction prevents large particles from passing and also regulates the amount of water that can pass through the transmembrane space at any given time. Our worlflow allows us to calculate the pore diameter at this constriction. Recent advances in pore diameter characterization of aquaporin complexes, from manipulation of molecular modeling files to visualization of results, will be presented here. References [1] V. Jalili et al., « The Galaxy platform for accessible, reproducible and collaborative biomedical analyses: 2020 up- date », Nucleic Acids Research, vol. 48, n o W1, p. W395-W402, juill. 2020, doi: 10.1093/nar/gkaa434. [2] R. O. Dror, R. M. Dirks, J. P. Grossman, H. Xu, et D. E. Shaw, « Biomolecular Simulation: A Computational Mi- croscope for Molecular Biology », Annu. Rev. Biophys., vol. 41, n o 1, p. 429-452, juin 2012, doi: 10.1146/annurev- biophys-042910-155245. [3] J.-S. Venisse et al., « Genome-Wide Identification, Structure Characterization, and Expression Pattern Profiling of the Aquaporin Gene Family in Betula pendula », IJMS, vol. 22, n o 14, p. 7269, juill. 2021, doi: 10.3390/ ijms22147269.