Magnesium in PDB 1nip: Crystallographic Structure of the Nitrogenase Iron Protein From Azotobacter Vinelandii

The structure of Crystallographic Structure of the Nitrogenase Iron Protein From Azotobacter Vinelandii, PDB code: 1nip was solved by H.Komiya, M.M.Georgiadis, P.Chakrabarti, D.Woo, J.J.Kornuc, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.800, 92.900, 63.600, 90.00, 100.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Crystallographic Structure of the Nitrogenase Iron Protein From Azotobacter Vinelandii also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Magnesium atom in the Crystallographic Structure of the Nitrogenase Iron Protein From Azotobacter Vinelandii (pdb code 1nip). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystallographic Structure of the Nitrogenase Iron Protein From Azotobacter Vinelandii, PDB code: 1nip:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystallographic Structure of the Nitrogenase Iron Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystallographic Structure of the Nitrogenase Iron Protein From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg291 b:10.6 occ:0.50 O A:HOH5013 1.8 17.9 0.5 O B:HOH5012 1.8 12.2 0.5 O B:HOH5014 1.8 5.0 0.5 O A:HOH5011 1.8 9.7 0.5 O3B B:ADP292 2.6 29.0 0.5 OG A:SER16 2.6 25.0 1.0 PB B:ADP292 3.2 29.0 0.5 O1B B:ADP292 3.2 29.0 0.5 N A:GLY14 3.3 13.0 1.0 CA A:GLY14 3.4 27.9 1.0 O2B B:ADP292 3.5 29.0 0.5 C A:GLY14 3.7 10.5 1.0 N A:LYS15 3.9 5.0 1.0 N A:SER16 3.9 5.0 1.0 CB A:SER16 4.0 32.1 1.0 O A:GLY14 4.2 5.0 1.0 N A:ILE13 4.4 29.7 1.0 C A:ILE13 4.5 13.0 1.0 CA A:SER16 4.5 22.9 1.0 N A:GLY12 4.6 5.0 1.0 CB A:ALA42 4.6 43.4 1.0 N A:THR17 4.7 5.0 1.0 CA A:GLY12 4.7 13.8 1.0 CA A:LYS15 4.7 5.0 1.0 C A:LYS15 4.7 5.0 1.0 CB A:LYS15 4.8 7.3 1.0 O3A B:ADP292 4.8 29.0 0.5 C A:GLY12 4.8 33.2 1.0

Magnesium binding site 2 out of 2 in the Crystallographic Structure of the Nitrogenase Iron Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystallographic Structure of the Nitrogenase Iron Protein From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg291 b:26.4 occ:0.50 O B:HOH5028 1.8 9.1 0.5 O B:HOH5027 1.8 8.0 0.5 O B:HOH5025 1.8 34.1 0.5 O B:HOH5026 1.8 5.0 0.5 OG B:SER16 2.9 36.1 1.0 C B:GLY14 3.6 19.0 1.0 N B:SER16 3.6 14.0 1.0 CA B:GLY14 3.7 15.4 1.0 N B:LYS15 3.7 24.1 1.0 N B:GLY14 3.8 24.1 1.0 O B:GLY14 3.9 23.3 1.0 CB B:SER16 4.1 39.5 1.0 CB B:LYS15 4.3 9.1 1.0 CA B:LYS15 4.4 22.0 1.0 CA B:SER16 4.4 27.1 1.0 OG1 B:THR17 4.4 42.5 1.0 C B:LYS15 4.5 27.3 1.0 N B:GLY12 4.5 32.4 1.0 CB B:ALA42 4.5 43.1 1.0 N B:THR17 4.7 29.1 1.0 N B:ILE13 4.9 47.5 1.0 C B:ILE13 4.9 37.0 1.0 CA B:GLY12 5.0 41.9 1.0

M.M.Georgiadis, H.Komiya, P.Chakrabarti, D.Woo, J.J.Kornuc, D.C.Rees. Crystallographic Structure of the Nitrogenase Iron Protein From Azotobacter Vinelandii. Science V. 257 1653 1992.
ISSN: ISSN 0036-8075
PubMed: 1529353