Magnesium in PDB 3aek: Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark

The structure of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark, PDB code: 3aek was solved by N.Muraki, J.Nomata, T.Shiba, Y.Fujita, G.Kurisu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.06 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.596, 81.219, 175.928, 90.00, 100.86, 90.00
R / Rfree (%)	19.1 / 23.2

The structure of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark also contains other interesting chemical elements:

Iron

(Fe)

8 atoms

The binding sites of Magnesium atom in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark (pdb code 3aek). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark, PDB code: 3aek:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg526 b:36.5 occ:1.00 MG B:PMR526 0.0 36.5 1.0 ND B:PMR526 1.9 36.6 1.0 NB B:PMR526 1.9 36.9 1.0 NC B:PMR526 2.0 36.9 1.0 NA B:PMR526 2.0 36.0 1.0 O B:HOH762 2.1 28.4 1.0 C4D B:PMR526 2.9 36.8 1.0 C4A B:PMR526 2.9 36.3 1.0 C1B B:PMR526 2.9 37.0 1.0 C1C B:PMR526 3.0 37.2 1.0 C4B B:PMR526 3.0 36.8 1.0 C4C B:PMR526 3.0 37.2 1.0 C1D B:PMR526 3.0 36.3 1.0 C1A B:PMR526 3.0 36.0 1.0 CHB B:PMR526 3.3 36.8 1.0 CHC B:PMR526 3.3 36.9 1.0 CHD B:PMR526 3.4 37.0 1.0 CHA B:PMR526 3.4 36.4 1.0 O B:HOH728 4.1 40.1 1.0 C2B B:PMR526 4.1 36.5 1.0 C3A B:PMR526 4.1 35.4 1.0 C3D B:PMR526 4.1 36.5 1.0 C3B B:PMR526 4.2 37.0 1.0 C2C B:PMR526 4.2 38.0 1.0 C2D B:PMR526 4.2 36.3 1.0 C2A B:PMR526 4.2 35.5 1.0 C3C B:PMR526 4.2 37.6 1.0 CD2 C:LEU372 4.2 37.6 1.0 O C:ALA57 4.5 54.3 1.0 O C:ALA58 4.8 57.6 1.0 CD1 C:ILE389 4.8 42.5 1.0 CBD B:PMR526 4.9 36.7 1.0 CG B:LEU410 5.0 59.6 1.0

Magnesium binding site 2 out of 2 in the Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Light-Independent Protochlorophyllide Reductase Catalyzing A Key Reduction For Greening in the Dark within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg526 b:35.7 occ:1.00 MG D:PMR526 0.0 35.7 1.0 NB D:PMR526 1.9 35.4 1.0 ND D:PMR526 1.9 35.6 1.0 NC D:PMR526 2.0 35.4 1.0 NA D:PMR526 2.0 34.3 1.0 O D:HOH597 2.1 41.7 1.0 C4D D:PMR526 2.9 35.0 1.0 C4A D:PMR526 2.9 34.4 1.0 C1B D:PMR526 3.0 35.2 1.0 C4B D:PMR526 3.0 35.3 1.0 C1C D:PMR526 3.0 35.1 1.0 C1A D:PMR526 3.0 34.3 1.0 C1D D:PMR526 3.0 35.3 1.0 C4C D:PMR526 3.0 35.7 1.0 CHC D:PMR526 3.3 35.0 1.0 CHB D:PMR526 3.3 34.6 1.0 CHA D:PMR526 3.4 34.9 1.0 CHD D:PMR526 3.4 35.2 1.0 CD2 A:LEU372 3.8 35.6 1.0 C2B D:PMR526 4.1 35.5 1.0 C3A D:PMR526 4.1 34.0 1.0 C3B D:PMR526 4.1 35.7 1.0 C3D D:PMR526 4.2 34.7 1.0 C2C D:PMR526 4.2 35.4 1.0 C2D D:PMR526 4.2 35.1 1.0 C2A D:PMR526 4.2 33.8 1.0 O D:HOH767 4.2 39.7 1.0 C3C D:PMR526 4.2 35.4 1.0 O A:ALA57 4.7 48.4 1.0 O A:ALA58 4.7 52.2 1.0 CD1 A:ILE389 4.8 41.2 1.0 CBD D:PMR526 4.9 35.2 1.0 CG D:LEU410 4.9 55.4 1.0

N.Muraki, J.Nomata, K.Ebata, T.Mizoguchi, T.Shiba, H.Tamiaki, G.Kurisu, Y.Fujita. X-Ray Crystal Structure of the Light-Independent Protochlorophyllide Reductase Nature V. 465 110 2010.
ISSN: ISSN 0028-0836
PubMed: 20400946
DOI: 10.1038/NATURE08950