Aminoacyl-tRNA synthetases (ARSs) are the essential enzymes linking amino acids to tRNAs for protein synthesis. Interestingly, mammalian ARSs play critical additional roles in diverse cellular pathways through the interactions with many other cellular factors. Among many ARS-containing complexes, the most intriguing one is the multi-tRNA synthetase complex consiting of nine different ARSs and three auxiliary factors called, AIMP1/p43, AIMP2/p38 and AIMP3/p18. Although the presence of this complex was known for decades, its three dimensional structure has not been solved. Here we propose the imaginary 3D structure of this complex based on electron microscopic structure of the complex, X-ray and NMR-based structures of the components and 3D modeling.