1.3.1.33	?	x * 36000, SDS-PAGE, x * 36046, calculated, S-tagged L-protein, x * 52000, SDS-PAGE, x * 48671, calculated, S-tagged N-protein, x * 60000, SDS-PAGE, x * 57191, calculated, B-protein	672324	
1.3.1.33	?	x * 37000, SDS-PAGE	741184	
1.3.1.33	?	x * 40150, recombinant enzyme, SDS-PAGE	654419	
1.3.1.33	?	x * 42500, isoform POR1, SDS-PAGE	741255	
1.3.1.33	?	x * 44000, isoform POR2, SDS-PAGE	741255	
1.3.1.33	?	x * 46000, precursor protein, x * 38000, mature protein	676012	
1.3.1.33	?	x * 47000, isoform POR1, calculated from amino acid sequence	741255	
1.3.1.33	?	x * 61000, isoform POR2, calculated from amino acid sequence	741255	
1.3.1.33	dimer	-	763650	
1.3.1.33	dimer	2 * 45000, SDS-PAGE	393836	
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	dimer	POR proteins in Arabidopsis consist of dimers	725793	
1.3.1.33	dimer	recombinant fusion protein, gel filtration	393856	
1.3.1.33	heterotetramer	2 * 46199 + 2 * 58729, purified ChlNB complex, deduced from amino acid sequence	687767	
1.3.1.33	homodimer	2 * 32395, purified ChlL subunit, deduced from amino acid sequence	687767	
1.3.1.33	monomer	1 * 36000, SDS-PAGE	393833, 393840	
1.3.1.33	monomer	the structure of enzyme (POR) protein is predicted in its monomeric and dimeric form	763675	
1.3.1.33	additional information	recombinant enzyme component L-protein forms a dimer, recombinant components NB-protein form a heterotetramer, gel filtration	672324	
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	barley PORA can form a five-unit oligomer that interacts with a single PORB	725793	
1.3.1.33	oligomer	oligomeric PORA-PORB complex	700943	
1.3.1.33	oligomer	protochlorophyllide binding triggers formation of large oligomers of the enzyme (POR). Oligomer formation is most likely driven by the interaction of amino acid residues in the highly conserved lid regions. The lid residues position protochlorophyllide optimally to enable photocatalysis. Following protochlorophyllide binding, they also enable POR oligomerisation - a process that is reversed through subsequent photocatalysis in the early stages of chloroplast development	763023