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Figure 4 | BMC Bioinformatics

Figure 4

From: Characterization of the cofactor-binding site in the SPOUT-fold methyltransferases by computational docking of S-adenosylmethionine to three crystal structures

Figure 4

Lowest-energy docking solutions obtained for a) 1gz0, b) 1ipa, c) 1k3r. AdoMet and selected important residues are shown in the wireframe representation and labeled. The label for the invariant Arg side chain, provided by the second monomer, is boxed. The rest of the protein is shown in a schematic representation (brown helices, green strands and purple loops). Selected sidechains are colored according to their physicochemical properties (Arg and Lys – blue; Glu – red; Thr and Ser – green; aliphatic (Pro, Val, Leu) – gray; Gly – cyan). For the residues that bind the cofactor and for the cofactor itself, the following color scheme is used: C – white, O – red, N – blue, S – yellow). Predicted hydrogen bonds are shown as green broken lines.

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BMC Bioinformatics

ISSN: 1471-2105

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