Magnesium in PDB 7ocr: Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii

The structure of Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocr 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)	48.71 / 2.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.886, 157.556, 220.467, 90, 90, 90
R / Rfree (%)	23 / 25.8

The structure of Nadph and Fructose-6-Phosphate 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
Potassium	(K)	1 atom

The binding sites of Magnesium atom in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii (pdb code 7ocr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Nadph and Fructose-6-Phosphate Bound to the Dehydrogenase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Nadph and Fructose-6-Phosphate 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 Nadph and Fructose-6-Phosphate 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:Mg814 b:60.4 occ:1.00 O A:ASP18 2.3 58.5 1.0 OD2 A:ASP16 2.3 56.8 1.0 OD1 A:ASP176 2.4 60.6 1.0 CG A:ASP16 3.3 56.0 1.0 CG A:ASP176 3.4 61.3 1.0 OE2 A:GLU175 3.5 60.5 1.0 O4 A:SO4801 3.5 108.8 1.0 C A:ASP18 3.5 59.0 1.0 OD2 A:ASP176 3.6 62.8 1.0 OD1 A:ASP16 3.7 56.7 1.0 O3 A:SO4801 4.2 108.0 1.0 OG A:SER177 4.3 60.8 1.0 CB A:SER177 4.3 61.5 1.0 S A:SO4801 4.4 108.6 1.0 CA A:ASP18 4.4 59.5 1.0 N A:GLY19 4.4 58.9 1.0 OE2 A:GLU25 4.5 67.4 1.0 N A:SER177 4.5 60.4 1.0 CA A:GLY19 4.5 58.9 1.0 N A:ASP18 4.6 58.5 1.0 CB A:ASP18 4.6 61.0 1.0 CB A:ASP16 4.6 54.8 1.0 CD A:GLU175 4.7 59.2 1.0 CB A:ASP176 4.7 60.3 1.0 OG1 A:THR20 4.7 55.1 1.0 O1 A:SO4801 4.9 108.5 1.0 N A:ASP176 5.0 58.9 1.0

Magnesium binding site 2 out of 2 in the Nadph and Fructose-6-Phosphate 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 Nadph and Fructose-6-Phosphate 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:Mg808 b:88.8 occ:1.00 O B:ASP18 2.5 111.5 1.0 OD2 B:ASP16 2.5 110.6 1.0 OD1 B:ASP176 2.6 112.5 1.0 O B:HOH902 3.1 84.9 1.0 OE2 B:GLU175 3.1 114.4 1.0 CG B:ASP16 3.4 109.7 1.0 OE1 B:GLU25 3.4 122.1 1.0 CG B:ASP176 3.6 113.1 1.0 OD1 B:ASP16 3.6 110.3 1.0 C B:ASP18 3.7 109.6 1.0 CA B:GLY54 3.7 125.3 1.0 OD2 B:ASP176 3.9 114.5 1.0 OG B:SER177 3.9 120.4 1.0 N B:GLY54 4.0 126.6 1.0 CB B:ASP18 4.2 111.1 1.0 CD B:GLU175 4.3 113.7 1.0 CB B:SER177 4.3 121.9 1.0 CA B:ASP18 4.4 108.5 1.0 N B:ASP18 4.6 106.8 1.0 CD B:GLU25 4.6 122.7 1.0 N B:SER177 4.7 117.8 1.0 CB B:ASP16 4.8 107.6 1.0 N B:GLY19 4.8 108.5 1.0 OE1 B:GLU175 4.9 112.5 1.0 CB B:ASP176 5.0 112.1 1.0 NZ B:LYS151 5.0 116.0 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