EC Number   |
Subunits |
Reference |
|---|
    1.3.1.33 | dimer |
- |
763650 |
| 1.3.1.33 | monomer |
1 * 36000, SDS-PAGE |
393833, 393840 |
| 1.3.1.33 | homodimer |
2 * 32395, purified ChlL subunit, deduced from amino acid sequence |
687767 |
| 1.3.1.33 | dimer |
2 * 45000, SDS-PAGE |
393836 |
| 1.3.1.33 | heterotetramer |
2 * 46199 + 2 * 58729, purified ChlNB complex, deduced from amino acid sequence |
687767 |
| 1.3.1.33 | oligomer |
barley PORA can form a five-unit oligomer that interacts with a single PORB |
725793 |
| 1.3.1.33 | dimer |
dimerization and binding of ligands (both the cofactor NADPH and substrate protochlorophyllide) are computationally investigated the sequence and structural relationships among homologous proteins are identified through database searches. The results indicate that alpha4 and alpha7 helices of monomers form the interface of NADPH:protochlorophyllide oxidoreductase dimers. On the basis of conserved residues, 11 functionally important amino acids that play important roles in binding of the enzyme to NADPH are predicted |
763675 |
| 1.3.1.33 | octamer |
heterooctameric complex: subunits N and B are structurally homologous, generating a pseudo-2fold symmetry axis that is colinear with the molecular twofold axis of L2. Both [4Fe-4S] clusters are centered around this extended axis: the L2 cluster is symmetrically ligated by four cysteinyl ligands between the two subunits, whereas the NB cluster is asymmetrically ligated by three cysteine residues from N and one aspartate residue from B |
726394 |
| 1.3.1.33 | oligomer |
oligomeric PORA-PORB complex |
700943 |
| 1.3.1.33 | dimer |
POR proteins in Arabidopsis consist of dimers |
725793 |
