EC Number   |
Subunits |
Reference |
|---|
   1.3.7.12 | ? |
x * 35000, precursor enzyme, SDS-PAGE, x * 31000, mature enzyme, SDS-PAGE |
735438 |
| 1.3.7.12 | dimer |
2 * 31000, SDS-PAGE |
676490 |
| 1.3.7.12 | homodimer |
2 * 32000, about, sequence calculation |
699585 |
| 1.3.7.12 | homodimer |
2 * 32000, predicted by amino acid sequence, each subunit folds in an alpha/beta/alpha sandwich |
699585 |
| 1.3.7.12 | homodimer |
RCCR folds into a characteristic alphabetaalpha sandwich |
712769 |
| 1.3.7.12 | More |
enzyme RCCR forms a homodimer, in which each subunit folds in an alphabetaalpha sandwich, five N-terminal alpha-helices (H1/H2/H3/H5/H7), an anti-parallel beta-sheet consisting of eight strands (S1-S8), and four C-terminal alpha-helices (H4/H6/H8/H9). The two subunits are related by noncrystallographic 2fold symmetry in which the alpha-helices near the edge of the beta-sheet unique in RCCR participate in intersubunit interaction. The putative RCC-binding site forms an open pocket surrounded by conserved residues among RCCRs. Residues Glu154 and Asp291 stand opposite each other in the substrate binding pocket and are likely involved in substrate binding and/or catalysis. Primary structure comparisons, overview |
699585 |
| 1.3.7.12 | More |
RCCR folds into a characteristic alpha/beta/alpha sandwich, similar to that observed in the ferredoxin-dependent bilin reductase family, structure comparisosns, overview |
712769 |
