EC Number |
Subunits |
Reference |
---|
1.1.1.282 | dimer |
- |
-, 644536, 739956 |
1.1.1.282 | dimer |
2 * 31350, wild type enzyme, gel filtration |
656292 |
1.1.1.282 | dimer |
distinct mode of dimerization in which the individual molecules interact in a back-to-front manner, overview. The molecules of the RifI2 dimer associate via hydrophobic interactions between residues on alpha-helix alpha8 of the first molecule and alpha10' of the second molecule. In addition, the side chain of Gln167 on apha-helix alpha8 forms a hydrogen bond with the guanidinium group of Arg243' on beta-strand beta10'. A second hydrogen bond to Arg243' may be made by Asn171. Asp53 and Arg56 on alpha-helix alpha2 bind the imidazole ring of His31' on alpha-helix alpha1' |
-, 740100 |
1.1.1.282 | homodimer |
- |
644537 |
1.1.1.282 | homodimer |
2 * 30000, about, recombinant enzyme, SDS-PAGE |
-, 724089 |
1.1.1.282 | monomer |
1 * 31500, SDS-PAGE |
-, 654384 |
1.1.1.282 | monomer |
1 * 41000 |
286356 |
1.1.1.282 | More |
enzyme three-dimensional structure determination, analysis, and comparisons, overview. The N-terminal or catalytic domain comprises residues 1 to 113 and 256 to 283, whereas the C-terminal or nucleotide-binding domain is build up of residues 114 to 255. The catalytic domain forms an open alpha/beta sandwich, which is characteristic for enzymes of the SDH/QDH family. The substrate-binding site is located in the N-terminal domain, close to the nicotinamide ring of the cofactor |
-, 727115 |