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

The structure of Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocp 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)	48.59 / 2.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.661, 157.692, 219.289, 90, 90, 90
R / Rfree (%)	22 / 25.5

The structure of Nadph 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)

2 atoms

The binding sites of Magnesium atom in the Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii (pdb code 7ocp). 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 Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocp:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Nadph 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 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:57.3 occ:1.00 OD2 A:ASP16 2.4 61.8 1.0 OD1 A:ASP176 2.4 67.8 1.0 O A:ASP18 2.5 64.1 1.0 O4 A:SO4803 3.2 98.0 1.0 CG A:ASP176 3.3 68.0 1.0 CG A:ASP16 3.3 61.3 1.0 OE2 A:GLU175 3.3 68.2 1.0 OD2 A:ASP176 3.5 69.7 1.0 OD1 A:ASP16 3.6 62.4 1.0 C A:ASP18 3.7 64.2 1.0 OG A:SER177 4.1 65.7 1.0 CB A:SER177 4.2 66.7 1.0 O1 A:SO4803 4.2 97.1 1.0 S A:SO4803 4.3 97.3 1.0 N A:SER177 4.4 65.7 1.0 OE2 A:GLU25 4.5 73.0 1.0 CD A:GLU175 4.6 66.7 1.0 CB A:ASP16 4.6 60.1 1.0 CA A:ASP18 4.6 64.7 1.0 CB A:ASP176 4.7 66.5 1.0 N A:GLY19 4.7 63.9 1.0 OG1 A:THR20 4.7 60.0 1.0 N A:ASP18 4.7 63.7 1.0 CA A:GLY19 4.8 63.2 1.0 CB A:ASP18 4.8 66.2 1.0 N A:ASP176 4.8 65.0 1.0 O3 A:SO4803 4.8 98.5 1.0 CA A:SER177 4.9 66.2 1.0

Magnesium binding site 2 out of 2 in the Nadph 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 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:Mg1004 b:89.7 occ:1.00 OD2 B:ASP16 2.4 122.2 1.0 O B:ASP18 2.5 123.9 1.0 OD1 B:ASP176 2.6 126.4 1.0 OE2 B:GLU175 3.1 126.2 1.0 OE1 B:GLU25 3.3 133.8 1.0 CG B:ASP16 3.4 120.6 1.0 CG B:ASP176 3.6 127.2 1.0 CA B:GLY54 3.6 136.2 1.0 C B:ASP18 3.7 122.1 1.0 OD1 B:ASP16 3.7 121.0 1.0 OG B:SER177 3.8 134.7 1.0 OD2 B:ASP176 3.8 128.8 1.0 CB B:ASP18 3.9 123.9 1.0 N B:GLY54 4.0 137.9 1.0 CB B:SER177 4.0 136.4 1.0 CA B:ASP18 4.2 121.0 1.0 CD B:GLU175 4.3 125.5 1.0 N B:SER177 4.4 132.2 1.0 CD B:GLU25 4.4 134.3 1.0 N B:ASP18 4.5 118.4 1.0 CB B:ASP16 4.7 118.2 1.0 NZ B:LYS151 4.7 128.1 1.0 N B:GLY19 4.8 121.0 1.0 CG B:GLU25 4.8 132.1 1.0 CA B:SER177 4.9 136.1 1.0 OG1 B:THR20 4.9 118.5 1.0 CB B:ASP176 4.9 126.4 1.0 N B:ASP176 5.0 125.3 1.0 C B:GLY54 5.0 138.6 1.0 OE1 B:GLU175 5.0 123.9 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