Magnesium in PDB 7oct: Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld-N374A From Acinetobacter Baumannii

The structure of Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld-N374A From Acinetobacter Baumannii, PDB code: 7oct 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)	48.43 / 2.85
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.304, 156.957, 220.028, 90, 90, 90
R / Rfree (%)	22.7 / 27.8

The structure of Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld-N374A From Acinetobacter Baumannii also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Potassium	(K)	1 atom

The binding sites of Magnesium atom in the Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld-N374A From Acinetobacter Baumannii (pdb code 7oct). 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-N374A From Acinetobacter Baumannii, PDB code: 7oct:
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-N374A 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-N374A From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg802 b:53.6 occ:1.00 OD2 A:ASP16 2.4 51.4 1.0 OD1 A:ASP176 2.4 55.1 1.0 O A:ASP18 2.4 52.9 1.0 O A:HOH917 2.9 38.1 1.0 OE2 A:GLU175 3.3 54.2 1.0 CG A:ASP176 3.4 55.3 1.0 CG A:ASP16 3.4 50.9 1.0 OD2 A:ASP176 3.6 56.8 1.0 C A:ASP18 3.7 53.1 1.0 OD1 A:ASP16 3.7 51.6 1.0 OG A:SER177 4.0 57.0 1.0 CB A:SER177 4.1 57.4 1.0 O A:HOH942 4.2 32.5 1.0 N A:SER177 4.4 55.5 1.0 O A:HOH920 4.5 46.9 1.0 O A:HOH948 4.5 43.2 1.0 CD A:GLU175 4.5 53.4 1.0 N A:GLY19 4.6 52.7 1.0 OE2 A:GLU25 4.6 59.8 1.0 CA A:ASP18 4.6 53.8 1.0 CA A:GLY19 4.6 52.3 1.0 CB A:ASP16 4.7 49.5 1.0 OG1 A:THR20 4.7 48.6 1.0 CB A:ASP176 4.7 54.3 1.0 CB A:ASP18 4.7 55.5 1.0 N A:ASP18 4.8 52.7 1.0 CA A:SER177 4.8 56.7 1.0 N A:ASP176 4.9 53.0 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-N374A 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-N374A From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1202 b:78.1 occ:1.00 O3 B:SO41203 2.1 134.3 1.0 OD1 B:ASP176 2.5 109.5 1.0 OD2 B:ASP16 2.5 109.8 1.0 OE2 B:GLU175 2.9 111.2 1.0 O B:ASP18 2.9 109.0 1.0 OG B:SER177 3.3 117.6 1.0 CG B:ASP16 3.4 108.8 1.0 CG B:ASP176 3.5 110.4 1.0 S B:SO41203 3.5 134.9 1.0 CB B:SER177 3.7 119.1 1.0 CA B:GLY54 3.7 122.0 1.0 OD1 B:ASP16 3.7 110.1 1.0 OE1 B:GLU25 3.7 115.0 1.0 OD2 B:ASP176 3.8 112.1 1.0 N B:SER177 4.0 115.1 1.0 N B:GLY54 4.0 123.2 1.0 CD B:GLU175 4.0 110.5 1.0 O1 B:SO41203 4.1 134.2 1.0 C B:ASP18 4.2 107.2 1.0 O4 B:SO41203 4.2 133.6 1.0 O2 B:SO41203 4.4 135.1 1.0 CA B:SER177 4.5 118.7 1.0 N B:ASP176 4.6 108.9 1.0 CB B:ASP16 4.7 106.3 1.0 OG1 B:THR20 4.7 103.4 1.0 CB B:ASP176 4.7 109.4 1.0 CG B:GLU175 4.8 111.4 1.0 CD B:GLU25 4.8 115.0 1.0 CB B:ASP18 4.8 109.5 1.0 OE1 B:GLU175 4.9 109.3 1.0 CA B:ASP18 4.9 106.6 1.0 NZ B:LYS151 4.9 112.4 1.0 C B:ASP176 5.0 113.9 1.0 C B:LEU53 5.0 125.9 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