Magnesium in PDB 6u44: Crystal Structure of Methanoperedens Nitroreducens Elongation Factor 2 H595N Bound to Gmppcp and Magnesium (Monoclinic Crystal Form)

The structure of Crystal Structure of Methanoperedens Nitroreducens Elongation Factor 2 H595N Bound to Gmppcp and Magnesium (Monoclinic Crystal Form), PDB code: 6u44 was solved by M.K.Fenwick, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	75.49 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	78.322, 106.814, 98.056, 90.00, 105.46, 90.00
R / Rfree (%)	18.7 / 24

The structure of Crystal Structure of Methanoperedens Nitroreducens Elongation Factor 2 H595N Bound to Gmppcp and Magnesium (Monoclinic Crystal Form) also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Magnesium atom in the Crystal Structure of Methanoperedens Nitroreducens Elongation Factor 2 H595N Bound to Gmppcp and Magnesium (Monoclinic Crystal Form) (pdb code 6u44). 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 Methanoperedens Nitroreducens Elongation Factor 2 H595N Bound to Gmppcp and Magnesium (Monoclinic Crystal Form), PDB code: 6u44:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Methanoperedens Nitroreducens Elongation Factor 2 H595N Bound to Gmppcp and Magnesium (Monoclinic Crystal Form)


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 Methanoperedens Nitroreducens Elongation Factor 2 H595N Bound to Gmppcp and Magnesium (Monoclinic Crystal Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg802 b:26.6 occ:1.00 O A:HOH982 2.0 19.5 1.0 O A:HOH947 2.0 27.2 1.0 OG1 A:THR71 2.0 31.8 1.0 O2G A:GCP801 2.1 23.8 1.0 OG1 A:THR35 2.1 34.5 1.0 O1B A:GCP801 2.1 31.6 1.0 CB A:THR71 3.1 29.1 1.0 CB A:THR35 3.2 30.1 1.0 PG A:GCP801 3.3 28.8 1.0 PB A:GCP801 3.3 25.2 1.0 C3B A:GCP801 3.5 27.4 1.0 N A:THR35 3.8 27.1 1.0 OD2 A:ASP60 4.0 33.6 1.0 N A:THR71 4.0 31.0 1.0 CA A:THR71 4.1 30.0 1.0 CA A:THR35 4.1 32.1 1.0 CG2 A:THR71 4.1 21.2 1.0 O1G A:GCP801 4.1 31.8 1.0 OD2 A:ASP94 4.2 34.1 1.0 OD1 A:ASP60 4.2 32.9 1.0 O2A A:GCP801 4.2 30.9 1.0 CE A:LYS34 4.3 20.1 1.0 O2B A:GCP801 4.3 19.6 1.0 OD1 A:ASP94 4.4 29.5 1.0 CG2 A:THR35 4.4 26.0 1.0 CB A:LYS34 4.4 20.1 1.0 O3G A:GCP801 4.4 27.0 1.0 O A:THR95 4.4 24.3 1.0 O3A A:GCP801 4.4 25.8 1.0 CG A:ASP60 4.5 32.6 1.0 O A:HOH917 4.6 40.5 1.0 CG A:ASP94 4.7 33.8 1.0 PA A:GCP801 4.7 28.2 1.0 C A:LYS34 4.8 29.8 1.0 NZ A:LYS34 4.9 18.5 1.0 O1A A:GCP801 4.9 29.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Methanoperedens Nitroreducens Elongation Factor 2 H595N Bound to Gmppcp and Magnesium (Monoclinic Crystal Form)


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 Methanoperedens Nitroreducens Elongation Factor 2 H595N Bound to Gmppcp and Magnesium (Monoclinic Crystal Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg802 b:30.0 occ:1.00 O2G B:GCP801 1.9 24.1 1.0 O B:HOH958 2.0 28.0 1.0 O1B B:GCP801 2.1 28.5 1.0 OG1 B:THR71 2.2 29.9 1.0 OG1 B:THR35 2.2 24.7 1.0 O B:HOH948 2.2 19.5 1.0 PG B:GCP801 3.0 30.3 1.0 CB B:THR71 3.1 24.7 1.0 PB B:GCP801 3.2 28.2 1.0 CB B:THR35 3.3 21.6 1.0 C3B B:GCP801 3.3 30.6 1.0 N B:THR35 3.9 25.9 1.0 O1G B:GCP801 4.0 29.7 1.0 N B:THR71 4.0 26.2 1.0 O2B B:GCP801 4.1 24.6 1.0 CA B:THR71 4.1 30.7 1.0 CA B:THR35 4.2 24.7 1.0 O3G B:GCP801 4.2 26.3 1.0 CG2 B:THR71 4.2 21.4 1.0 O2A B:GCP801 4.2 33.7 1.0 OD2 B:ASP60 4.3 32.3 1.0 CE B:LYS34 4.3 20.1 1.0 OD1 B:ASP60 4.3 28.8 1.0 OD2 B:ASP94 4.4 35.0 1.0 CB B:LYS34 4.4 19.3 1.0 O3A B:GCP801 4.4 25.3 1.0 O B:THR95 4.4 24.4 1.0 CG2 B:THR35 4.4 19.8 1.0 OD1 B:ASP94 4.4 31.0 1.0 PA B:GCP801 4.7 28.1 1.0 CG B:ASP60 4.7 30.3 1.0 C B:LYS34 4.8 23.2 1.0 CG B:ASP94 4.8 33.1 1.0 NZ B:LYS34 4.9 21.4 1.0 O B:HOH988 5.0 30.8 1.0

M.K.Fenwick, S.E.Ealick. Structural Basis of Elongation Factor 2 Switching Curr Res Struct Biol V. 2 25 2020.
ISSN: ESSN 2665-928X
DOI: 10.1016/J.CRSTBI.2020.02.001