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Figure 3 | BMC Structural Biology

Figure 3

From: Crystal structure of the signaling helix coiled-coil domain of the β1 subunit of the soluble guanylyl cyclase

Figure 3

Structure of CC of sGCβ1 and dimer analysis. A, Omit | Fo| -| Fc| electron density of the C-terminal end of the αB helix of molecule B, contoured at 2.5 σ. B, schematic diagram of asymmetric unit contents of CC of sGCβ1 revealing 2 CC tetramers. Shown are CC molecule A (red) with the long αA and short αB helix labeled, as well as molecules B (blue), C (yellow), D magenta, E (light red), F (light blue), G (light yellow), and H (light magenta). C, dimer interface calculations using PISA [26], D, different dimer interfaces and the presence or absence of water molecules (red crosses) between monomers. E, graph depicting Cα-Cα distance for αA residues from molecule A to either the nearest residue in molecule B (diamonds) or to molecule D (grey squares) that are shorter than 10 Å

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