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. 2001 Apr 10;98(9):5002–5006. doi: 10.1073/pnas.081072898

Figure 4.

Figure 4

Stereoview of heme groups (brown) and the intervening protein and solvent medium. Residues below (a) and above (b) the heme plane on the left-hand side are shown separately. The side- and main-chain atoms of 14 residues on each molecule participate in the interface, burying 400 Å2 of solvent-accessible surface area on Moli (green) and 360 Å2 on Moli+1 (gray). Close contacts (black traces) in the interface include those between Ile-81i and Ile-75i+1, and the heme vinyli and Lys-55i+1. The side chain of Lys-55i+1 and the peptide carbonyl of Ile-81i form the only direct protein–protein hydrogen bond (yellow traces). Water-bridged hydrogen bonds link the main chain of Phe-82i to that of Lys-73i+1, the side chain of Asp-16i to that of Lys-55i+1, and the main chain of Ile-81i to both the main and side chains of Lys-55i+1. A series of two or more water molecules (blue spheres) mediate additional hydrogen bonds between interfacial residues.