The current pandemic of the viral 2009 H1N1 influenza and its sustained human-human transmission has raised global concern for human health. The binding of the viral glycoprotein hemagglutinin (HA) and the human α-2,6-linked sialopentasaccharide (SIA-2,6-GAL) host cell receptor is a critical step in the viral replication cycle. Here, the complex structure of the 2009 H1N1 HA bound to the SIA-2,6-GAL sialopentasaccharide receptor was constructed by using homology modeling and molecular dynamic simulations. The receptor was found to fit very well within the HA binding pocket and formed hydrogen bonds with the residues of the 130-loop, 190-helix, and 220-loop. Most receptor binding residues play a significant role in stabilizing the protein-receptor complex with major contributions being provided by V135, T136, A137, K222, and Q226. The results are similar to the human SIA-2,6-GAL sialopentasaccharide receptor binding to H1 HA subtype, but are slightly different from those of H3, H5, and H9 HAs.