3AGC

F218V mutant of the substrate-bound red chlorophyll catabolite reductase from Arabidopsis thaliana

Summary for 3AGC

Entry DOI	10.2210/pdb3agc/pdb
Related	2ZXL 3AGA 3AGB
Descriptor	Red chlorophyll catabolite reductase, chloroplastic, 3-{(2Z,3S,4S)-5-[(Z)-(4-ethenyl-3-methyl-5-oxo-1,5-dihydro-2H-pyrrol-2-ylidene)methyl]-2-[(5R)-2-[(3-ethyl-5-formyl-4-methyl-1H-pyrrol-2-yl)methyl]-5-(methoxycarbonyl)-3-methyl-4-oxo-4,5-dihydrocyclopenta[b]pyrrol-6(1H)-ylidene]-4-methyl-3,4-dihydro-2H-pyrrol-3-yl}propanoic acid, SODIUM ION, ... (4 entities in total)
Functional Keywords	chlorophyll degradation, substrate-bound enzyme, chlorophyll catabolism, chloroplast, nadp, oxidoreductase, transit peptide
Biological source	Arabidopsis thaliana (mouse-ear cress, thale-cress)
Cellular location	Plastid, chloroplast stroma: Q8LDU4
Total number of polymer chains	2
Total formula weight	63368.21
Authors	Sugishima, M.,Fukuyama, K. (deposition date: 2010-03-30, release date: 2010-09-01, Last modification date: 2023-11-01)
Primary citation	Sugishima, M.,Okamoto, Y.,Noguchi, M.,Kohchi, T.,Tamiaki, H.,Fukuyama, K. Crystal structures of the substrate-bound forms of red chlorophyll catabolite reductase: implications for site-specific and stereospecific reaction J.Mol.Biol., 402:879-891, 2010 Cited by PubMed: 20727901 DOI: 10.1016/j.jmb.2010.08.021 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation