Figure 3
(a) The 2Fo − Fc σA-weighted electron-density map (shown in cyan) for the inhibitor 4,7-dioxosebacic acid at 2.60 Å resolution. The covalent bonds between the inhibitor and lysines 200 and 253 are also shown. (b) The hydrogen bonds made by the carboxyl groups of the inhibitor with surrounding residues (donor–acceptor distances are shown in Å). The atoms labelled C4 and C7 are attached to the invariant lysine residues by Schiff bases. In both (a) and (b) the map is contoured at 1.25 r.m.s. and the A-site of the enzyme is on the left-hand side, with the P-site on the right. |