Magnesium in PDB 7ocq: Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii

The structure of Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocq was solved by H.K.Tam, V.Mueller, K.M.Pos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.42 / 2.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.301, 157.337, 219.02, 90, 90, 90
R / Rfree (%)	23.2 / 28.8

The structure of Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii also contains other interesting chemical elements:

Chlorine

(Cl)

7 atoms

The binding sites of Magnesium atom in the Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii (pdb code 7ocq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocq:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg802 b:55.3 occ:1.00 OD2 A:ASP16 2.3 70.8 1.0 OD1 A:ASP176 2.3 73.9 1.0 O A:ASP18 2.4 75.2 1.0 O3 A:SO4803 3.1 107.1 1.0 CG A:ASP176 3.3 74.3 1.0 CG A:ASP16 3.3 70.8 1.0 OD2 A:ASP176 3.5 75.9 1.0 OE2 A:GLU175 3.6 74.0 1.0 C A:ASP18 3.6 74.8 1.0 OD1 A:ASP16 3.6 71.6 1.0 O1 A:SO4803 4.1 106.9 1.0 CB A:SER177 4.1 75.7 1.0 S A:SO4803 4.2 107.4 1.0 OG A:SER177 4.3 75.0 1.0 OE2 A:GLU25 4.3 83.0 1.0 N A:SER177 4.3 74.1 1.0 N A:GLY19 4.4 74.2 1.0 CA A:GLY19 4.5 73.5 1.0 CA A:ASP18 4.6 75.2 1.0 CB A:ASP16 4.6 69.8 1.0 CB A:ASP176 4.6 73.3 1.0 N A:ASP18 4.8 74.0 1.0 CD A:GLU175 4.8 73.0 1.0 CB A:ASP18 4.8 77.1 1.0 OG1 A:THR20 4.8 69.7 1.0 N A:ASP176 4.9 72.2 1.0 CA A:SER177 4.9 75.5 1.0 O4 A:SO4803 4.9 107.5 1.0

Magnesium binding site 2 out of 2 in the Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Nadh Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1- Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg804 b:92.4 occ:1.00 OD1 B:ASP176 2.4 129.2 1.0 O B:ASP18 2.5 125.2 1.0 OD2 B:ASP16 2.6 124.0 1.0 OE2 B:GLU175 3.2 128.4 1.0 CG B:ASP16 3.4 123.0 1.0 OE1 B:GLU25 3.4 132.7 1.0 CG B:ASP176 3.5 129.5 1.0 OD1 B:ASP16 3.5 123.7 1.0 CA B:GLY54 3.6 136.6 1.0 C B:ASP18 3.7 123.7 1.0 OD2 B:ASP176 3.8 131.0 1.0 OG B:SER177 4.0 134.9 1.0 N B:GLY54 4.0 137.8 1.0 CB B:SER177 4.1 135.9 1.0 CB B:ASP18 4.1 125.5 1.0 CA B:ASP18 4.3 122.8 1.0 NZ B:LYS151 4.4 128.9 1.0 CD B:GLU25 4.4 132.9 1.0 CD B:GLU175 4.4 128.1 1.0 N B:SER177 4.4 132.4 1.0 CG B:GLU25 4.6 130.5 1.0 N B:ASP18 4.6 121.0 1.0 N B:GLY19 4.8 122.5 1.0 CB B:ASP16 4.8 121.1 1.0 CB B:ASP176 4.8 128.1 1.0 CA B:SER177 4.9 135.4 1.0 N B:ASP176 5.0 127.2 1.0 C B:GLY54 5.0 138.8 1.0

H.K.Tam, P.Konig, S.Himpich, N.D.Ngu, R.Abele, V.Muller, K.M.Pos. Unidirectional Mannitol Synthesis of Acinetobacter Baumannii Mtld Is Facilitated By the Helix-Loop-Helix-Mediated Dimer Formation. Proc.Natl.Acad.Sci.Usa V. 119 94119 2022.
ISSN: ESSN 1091-6490
PubMed: 35363566
DOI: 10.1073/PNAS.2107994119