Over the past decade, structures have been determined for broadly neutralizing antibodies that recognize all major exposed surfaces of the prefusion-closed HIV-1-envelope (Env) trimer. To understand this recognition and its implications, we analyzed 206 antibody-HIV-1 Env structures from the Protein Data Bank with resolution suitable to define interaction chemistries and measured antibody neutralization on a 208-strain panel. Those with >25% breadth segregated into almost two dozen classes based on ontogeny and recognition and into six epitope categories based on recognized Env residues. For paratope, the number of protruding loops and level of somatic hypermutation were significantly higher for broad HIV-1 neutralizing antibodies than for a comparison set of non-HIV-1 antibodies (p < 0.0001). For epitope, the number of independent sequence segments was higher (p < 0.0001), as well as the glycan component surface area (p = 0.0005). The unusual characteristics of epitope and paratope delineated here are likely to reflect respectively virus-immune evasion and antibody-recognition solutions that allow effective neutralization of HIV-1. Display omitted •Classification of HIV-1 antibodies into six categories based on recognized epitope•Delineation of underlying relationships between neutralization and epitope/paratope•Identification of epitope/paratope features specific to HIV-1 antibodies•Evaluation of epitopes for ease of antibody elicitation by vaccination Antibody-envelope structures have been determined that recognize all major exposed surfaces of the HIV-1 envelope trimer. Chuang et al. classify these structures to delineate overall categories and to reveal underlying relationships between neutralization and epitope/paratope, specific features of HIV-1 broadly neutralizing antibodies, and sites of vulnerability most suitable for vaccine design.