Figure 2
From: The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata
(A) Stereo view of the 2mFo-DFc electron density map of apo-SeviL, showing the dimer interface created by the two-fold symmetry axis. Carbon atoms are shown in brown for one subunit and white for the other. Oxygen atoms are coloured red and nitrogen blue. Hydrogen bonds are shown as orange dotted lines. The Gln 12 side-chain forms a double hydrogen bond with its symmetry mate. The nitrogen atom of Met 36 donates a hydrogen bond to the oxygen atom of Arg 14 in the partner subunit. The map is contoured at 1 \(\sigma\). (B) The 2mFo-DFc electron density map covering the tetrasaccharide bound by SeviL. The glucose residue is more mobile, but the temperature factors and density for the other residues indicate high occupancy in a single conformation.
