Magnesium in PDB 5h92: Crystal Structure of the Complex Between Maize Sulfite Reductase and Ferredoxin in the Form-3 Crystal

All present enzymatic activity of Crystal Structure of the Complex Between Maize Sulfite Reductase and Ferredoxin in the Form-3 Crystal:
1.8.7.1;

The structure of Crystal Structure of the Complex Between Maize Sulfite Reductase and Ferredoxin in the Form-3 Crystal, PDB code: 5h92 was solved by G.Kurisu, M.Nakayama, T.Hase, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.27 / 2.08
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	103.414, 103.406, 122.434, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 23.2

The structure of Crystal Structure of the Complex Between Maize Sulfite Reductase and Ferredoxin in the Form-3 Crystal also contains other interesting chemical elements:

Iron

(Fe)

12 atoms

The binding sites of Magnesium atom in the Crystal Structure of the Complex Between Maize Sulfite Reductase and Ferredoxin in the Form-3 Crystal (pdb code 5h92). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Complex Between Maize Sulfite Reductase and Ferredoxin in the Form-3 Crystal, PDB code: 5h92:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Complex Between Maize Sulfite Reductase and Ferredoxin in the Form-3 Crystal


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Complex Between Maize Sulfite Reductase and Ferredoxin in the Form-3 Crystal within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg704 b:20.5 occ:1.00 O A:ASN453 2.6 24.3 1.0 ND2 A:ASN455 2.6 20.6 1.0 O A:HOH884 2.7 24.9 1.0 O A:VAL424 2.7 26.1 1.0 O A:HOH825 2.9 26.1 1.0 CG A:ASN455 3.3 24.6 1.0 O A:HOH874 3.4 22.4 1.0 OD1 A:ASN455 3.4 28.9 1.0 O A:GLN454 3.8 23.3 1.0 C A:VAL424 3.8 25.4 1.0 C A:ASN453 3.8 24.5 1.0 C A:GLN454 3.9 23.7 1.0 CB A:GLN454 4.2 20.8 1.0 O A:ALA491 4.2 24.3 1.0 N A:VAL424 4.3 24.9 1.0 ND1 A:HIS423 4.3 23.1 1.0 N A:ASN455 4.3 23.0 1.0 N A:ASN426 4.3 24.9 1.0 O A:HOH878 4.4 29.0 1.0 CE1 A:HIS423 4.4 25.3 1.0 CA A:GLN454 4.5 23.0 1.0 OE1 A:GLN454 4.5 24.9 1.0 CB A:ASN455 4.6 23.2 1.0 N A:GLN454 4.6 23.4 1.0 N A:ASP425 4.6 25.1 1.0 CA A:VAL424 4.6 24.5 1.0 CB A:ASN453 4.6 24.7 1.0 CA A:ASP425 4.6 25.6 1.0 CA A:ASN455 4.7 24.4 1.0 N A:GLY427 4.7 26.7 1.0 CA A:ASN453 4.8 25.5 1.0 C A:ASP425 4.8 25.9 1.0 O A:LEU489 5.0 24.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Complex Between Maize Sulfite Reductase and Ferredoxin in the Form-3 Crystal


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Complex Between Maize Sulfite Reductase and Ferredoxin in the Form-3 Crystal within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg704 b:22.4 occ:1.00 O B:HOH890 2.6 30.9 1.0 ND2 B:ASN455 2.7 21.1 1.0 O B:HOH832 2.7 30.0 1.0 O B:ASN453 2.7 26.6 1.0 O B:VAL424 2.7 27.9 1.0 O B:HOH843 3.3 29.9 1.0 CG B:ASN455 3.3 30.0 1.0 OD1 B:ASN455 3.4 29.8 1.0 C B:VAL424 3.8 29.7 1.0 C B:ASN453 3.9 26.8 1.0 O B:GLN454 3.9 25.8 1.0 C B:GLN454 4.1 25.3 1.0 O B:ALA491 4.2 27.4 1.0 ND1 B:HIS423 4.2 28.7 1.0 N B:VAL424 4.3 29.3 1.0 CB B:GLN454 4.3 25.9 1.0 O B:HOH818 4.3 31.7 1.0 N B:ASN426 4.4 29.9 1.0 CE1 B:HIS423 4.4 31.3 1.0 OE1 B:GLN454 4.5 27.9 1.0 N B:ASN455 4.5 26.0 1.0 CA B:GLN454 4.6 25.1 1.0 CB B:ASN455 4.6 26.5 1.0 CA B:VAL424 4.6 29.4 1.0 O B:LEU489 4.7 28.6 1.0 CB B:ASN453 4.7 28.0 1.0 N B:ASP425 4.7 29.9 1.0 CA B:ASP425 4.7 30.5 1.0 N B:GLN454 4.7 25.9 1.0 CA B:ASN455 4.8 27.0 1.0 N B:GLY427 4.8 28.7 1.0 CA B:ASN453 4.9 26.5 1.0 C B:ASP425 4.9 30.1 1.0 O B:ASN488 4.9 29.5 1.0

J.Y.Kim, M.Nakayama, H.Toyota, G.Kurisu, T.Hase. Structural and Mutational Studies of An Electron Transfer Complex of Maize Sulfite Reductase and Ferredoxin. J.Biochem. V. 160 101 2016.
ISSN: ISSN 0021-924X
PubMed: 26920048
DOI: 10.1093/JB/MVW016