3FWY
Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein
Replaces: 3ENDSummary for 3FWY
Entry DOI | 10.2210/pdb3fwy/pdb |
Descriptor | Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
Functional Keywords | bchl, protochlorophyllide, electron donor, dpor, fe protein, nitrogenase, mixed alpha-beta domain, mgadp, atp-binding, bacteriochlorophyll biosynthesis, chlorophyll biosynthesis, iron, iron-sulfur, metal-binding, nucleotide-binding, oxidoreductase, photosynthesis |
Biological source | Rhodobacter sphaeroides 2.4.1 |
Total number of polymer chains | 2 |
Total formula weight | 70284.74 |
Authors | Sarma, R.,Barney, B.M.,Hamilton, T.L.,Jones, A.,Seefeldt, L.C.,Peters, J.W. (deposition date: 2009-01-19, release date: 2009-03-24, Last modification date: 2023-09-06) |
Primary citation | Sarma, R.,Barney, B.M.,Hamilton, T.L.,Jones, A.,Seefeldt, L.C.,Peters, J.W. Crystal Structure of the L Protein of Rhodobacter sphaeroides Light-Independent Protochlorophyllide Reductase with MgADP Bound: A Homologue of the Nitrogenase Fe Protein. Biochemistry, 47:13004-13015, 2008 Cited by PubMed: 19006326DOI: 10.1021/bi801058r PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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