EC Number |
Subunits |
Reference |
---|
1.1.2.7 | tetramer |
2 * 65000 + 2 * 9000 |
-, 667721 |
1.1.2.7 | tetramer |
alpha2beta2 structure, subunit organization and structure, docking model, overview |
-, 667721 |
1.1.2.7 | ? |
x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE |
-, 670785 |
1.1.2.7 | More |
the periplasmic protein contains both a PQQ-containing domain, folded into a beta-propeller fold, and a smaller cytochrome c domain, which is analogous to a typical class I c-type cytochrome, these two domains are connected via a proline-rich linker region, which lacks any secondary structure, structure model of the electron-transfer complex formed by MDH and cytochrome cL, overview |
671068 |
1.1.2.7 | tetramer |
alpha2beta2 subunit conposition, structure model of an alphabeta unit from crystal structure determination, overview |
671068 |
1.1.2.7 | tetramer |
2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination |
-, 673047 |
1.1.2.7 | tetramer |
2 * 65000, alpha-subunit, + 2 * 9000, beta-subunit, SDS-PAGE |
-, 673048 |
1.1.2.7 | More |
the large alpha-subunit has a propeller fold making up a superbarrel of eight radially arranged beta-sheets, i.e. the propeller blades, containing the tryptophan-docking motifs that link together the eight beta-sheets, and the presence in the active site of a unique eight-membered disulfide ring structure formed from adjacent cysteine residues 103 and 104, joined by an atypical non-planar peptide bond |
684666 |
1.1.2.7 | tetramer |
2 * 66000 + 2 * 8500, alpha2beta2, crystal structure determination |
684666 |
1.1.2.7 | tetramer |
alpha2beta2, comparison of wild-type and mutant enzyme structures, overview |
-, 684947 |