1.2.1.105 | structure of the component E2 catalytic domain, to 3.0 A resolution using molecular replacement. The active site is located in the middle of a channel formed at the interface between two 3fold related subunits. Active-site residues are His375 and Thr323 and Asp379. Binding of the substrates to E2 catalytic domain is proposed to induce a change in the conformation of Asp379, allowing this residue to form a salt bridge with Arg 184. Residues Ser330, Ser333, and His348 form the succinyl-binding pocket |