Abstract Protein side chain packing (PSCP) is a fundamental problem in the field of protein engineering, as high‐confidence and low‐energy conformations of amino acid side chains are crucial for understanding (and designing) protein folding, protein–protein interactions, and protein‐ligand interactions. Traditional PSCP methods (such as the Rosetta Packer) often rely on a library of discrete side chain conformations, or rotamers, and a forcefield to guide the structure to low‐energy conformations. Recently, deep learning (DL) based methods (such as DLPacker, AttnPacker, and DiffPack) have demonstrated state‐of‐the‐art predictions and speed in the PSCP task. Building off the success of geometric graph neural networks for protein modeling, we present the Protein Invariant Point Packer (PIPPack) which effectively processes local structural and sequence information to produce realistic, idealized side chain coordinates using ‐angle distribution predictions and geometry‐aware invariant point message passing (IPMP). On a test set of ∼1400 high‐quality protein chains, PIPPack is highly competitive with other state‐of‐the‐art PSCP methods in rotamer recovery and per‐residue RMSD but is significantly faster.