The multitude of glycans on any cell surface can appear homogeneous overall, but a more site‐specific perspective suggests some deliberate diversity. Many have argued that site‐specific microheterogeneity arises from the influence of protein structure on glycan synthesis, yet, the prevailing consensus is that glycan synthesis is non‐template driven. We examine the possibility that the diversity of site‐specific glycoprofiles is a result of the affinity for glycosyltransferases to various regions of that protein. In this study, we examine an empirical glycoprotein database containing evidence of site‐specific glycosylation events. Each glycan substructures was correlated to site‐specific protein structure features (e.g. secondary structure, proximal amino acids). By characterizing correlations between glycan substructures and local protein chemistry, we have produced a draft template which we have applied to further our understanding of the HIV envelope mannosylation, predict temporospatial changes in flu glycosylation, explain discrepancies in amino acid substitutions matrices, predict TAPBP dependence in HLA, and predict secretion rates. In an attempt to share our advance, we are currently predicting glycosylation throughout PDB and SWISSMOD and identifying mutations in ClinVar most likely to be glycan‐modulated. By determining occlusion of GTs on structurally annotated sites, we can learn about the structural specificities of these impactful proteins thereby increasing our capacity to understand and predict their behavior.Support or Funding InformationNIH 1 R21 HD088953, NNF10CC1016517