5.1.1.13 | homodimer |
comparisons of Picrophilus torridus enzyme structure with the Pyrococcus aspartate racemase structure. The dimerization interface is composed of three interaction surfaces, including an inter-subunit disulfide bond and contacts through the beta-sheets and alpha-helix. The interface between two molecules (Mol-A and Mol-B) of Picrophilus torridus PtoAspR looks similar to that of Pyrococcus aspartate racemase, except that there is no cysteine disulfide bond between two molecules of PtoAspR. Each subunit is composed of two homologous domains, the N-terminal domain with residues 1-101 and 207-232, and the C-terminal domain with residues 106-206. The putative catalytic residues, Arg49, Cys83, Asn84, Thr85, Lys159, Cys188, Thr189, are located in the pocket between two domains |
-, 747720 |