VRC01-class broadly neutralizing antibodies (bnAbs) target the CD4-binding site (CD4BS) of the human immunodeficiency virus-1 (HIV-1) envelope glycoprotein (Env) and are of major interest for vaccine design. Unlike mature antibodies, corresponding VRC01-class germline precursors poorly bind to Env due to their weak ability to overcome the steric hindrance imparted by the glycans surrounding the CD4 BS. To date, immunogen design initiatives have largely relied on removal of these glycans and have met limited success in eliciting VRC01-class bnAbs. To understand elicitation of such bnAbs in humans, we structurally characterized the inferred germline precursor of VRC01 in complex with wild-type core gp120 by X-ray crystallography and modified trimeric 426c Env constructs by single-particle electron microscopy. We then validated glycan length and composition of germline VRC01-compatible Env constructs by EThcD LC-MS/MS. Our results reveal that engagement of the VRC01 germline antibody by a wild-type 426c gp120 is possible and can be enhanced by tailoring glycan length in the vicinity of the CD4BS.