Magnesium in PDB 3aeq: 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: 3aeq 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)	47.25 / 2.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.632, 81.278, 177.103, 90.00, 100.43, 90.00
R / Rfree (%)	23.5 / 29.8

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 3aeq). 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: 3aeq:
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:18.4 occ:0.50 MG B:PMR526 0.0 18.4 0.5 O B:HOH532 1.8 50.0 1.0 ND B:PMR526 1.9 18.3 0.5 NB B:PMR526 1.9 19.1 0.5 NC B:PMR526 2.0 17.7 0.5 NA B:PMR526 2.0 19.0 0.5 C4D B:PMR526 2.9 18.3 0.5 C4A B:PMR526 2.9 19.4 0.5 C1B B:PMR526 2.9 19.1 0.5 C1C B:PMR526 3.0 18.3 0.5 C4B B:PMR526 3.0 19.1 0.5 C1D B:PMR526 3.0 18.2 0.5 C4C B:PMR526 3.0 17.6 0.5 C1A B:PMR526 3.0 19.5 0.5 CHB B:PMR526 3.3 19.4 0.5 CHC B:PMR526 3.3 18.6 0.5 CHD B:PMR526 3.4 18.1 0.5 CHA B:PMR526 3.4 18.7 0.5 C3A B:PMR526 4.1 19.9 0.5 C2B B:PMR526 4.1 18.4 0.5 C3D B:PMR526 4.1 18.7 0.5 C3B B:PMR526 4.2 18.7 0.5 C2D B:PMR526 4.2 18.6 0.5 C2C B:PMR526 4.2 17.9 0.5 C2A B:PMR526 4.2 20.3 0.5 C3C B:PMR526 4.2 17.5 0.5 CD2 C:LEU372 4.4 53.2 1.0 CD1 B:LEU410 4.6 46.0 0.5 O C:ALA58 4.7 57.3 1.0 CBD B:PMR526 4.9 18.4 0.5 O C:ALA57 4.9 54.9 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:26.2 occ:0.50 MG D:PMR526 0.0 26.2 0.5 ND D:PMR526 1.9 26.6 0.5 NB D:PMR526 1.9 27.2 0.5 NA D:PMR526 2.0 25.8 0.5 NC D:PMR526 2.0 25.9 0.5 O A:HOH527 2.0 52.0 1.0 C4D D:PMR526 2.9 26.6 0.5 C4A D:PMR526 2.9 26.0 0.5 C1B D:PMR526 2.9 27.5 0.5 C1C D:PMR526 3.0 26.4 0.5 C4B D:PMR526 3.0 27.4 0.5 C1D D:PMR526 3.0 26.3 0.5 C4C D:PMR526 3.0 25.4 0.5 C1A D:PMR526 3.0 26.0 0.5 CHB D:PMR526 3.2 26.5 0.5 CHC D:PMR526 3.3 26.6 0.5 CHD D:PMR526 3.4 25.9 0.5 CHA D:PMR526 3.4 26.1 0.5 C2B D:PMR526 4.1 27.4 0.5 C3A D:PMR526 4.1 26.1 0.5 C3D D:PMR526 4.1 27.1 0.5 C3B D:PMR526 4.1 27.8 0.5 C2C D:PMR526 4.2 25.6 0.5 C2D D:PMR526 4.2 26.7 0.5 C3C D:PMR526 4.2 25.2 0.5 C2A D:PMR526 4.2 25.9 0.5 CD1 D:LEU410 4.5 46.9 0.5 CD2 A:LEU372 4.5 51.5 1.0 O A:ALA58 4.5 56.8 1.0 O A:ALA57 4.6 54.6 1.0 CBD D:PMR526 4.9 26.6 0.5

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