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

The structure of Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld- N374A From Acinetobacter Baumannii, PDB code: 7ocu 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)	48.49 / 2.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.439, 157.433, 219.824, 90, 90, 90
R / Rfree (%)	22.7 / 26.4

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

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld- N374A From Acinetobacter Baumannii (pdb code 7ocu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld- N374A From Acinetobacter Baumannii, PDB code: 7ocu:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Mannitol-1-Phosphate Bound to the Phosphatase 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 Mannitol-1-Phosphate Bound to the Phosphatase 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:66.2 occ:1.00 O A:ASP18 2.3 68.3 1.0 OD2 A:ASP16 2.3 66.5 1.0 OD1 A:ASP176 2.4 68.0 1.0 CG A:ASP176 3.3 68.7 1.0 O4 A:SO4803 3.3 123.2 1.0 CG A:ASP16 3.4 65.2 1.0 OD2 A:ASP176 3.5 70.6 1.0 C A:ASP18 3.5 68.6 1.0 OE2 A:GLU175 3.5 67.2 1.0 O3 A:SO4803 3.8 122.6 1.0 OD1 A:ASP16 3.9 65.9 1.0 O A:HOH903 4.2 75.9 1.0 S A:SO4803 4.2 123.4 1.0 N A:GLY19 4.4 68.0 1.0 OG A:SER177 4.4 70.2 1.0 CB A:SER177 4.4 70.9 1.0 CA A:GLY19 4.4 67.6 1.0 CA A:ASP18 4.5 69.5 1.0 N A:SER177 4.6 69.0 1.0 OE2 A:GLU25 4.6 80.0 1.0 CB A:ASP16 4.6 63.5 1.0 CB A:ASP18 4.7 71.6 1.0 CB A:ASP176 4.7 67.7 1.0 N A:ASP18 4.7 68.4 1.0 CD A:GLU175 4.7 66.0 1.0 N A:THR20 4.9 64.8 1.0 OG1 A:THR20 5.0 63.2 1.0 N A:ASP176 5.0 65.8 1.0

Magnesium binding site 2 out of 3 in the Mannitol-1-Phosphate Bound to the Phosphatase 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 Mannitol-1-Phosphate Bound to the Phosphatase 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:Mg804 b:66.3 occ:1.00 O A:HOH904 2.5 57.2 1.0 O A:HOH937 2.6 62.3 1.0 OD2 A:ASP223 3.7 56.2 1.0 O A:HOH922 3.9 50.6 1.0 CE2 A:TYR216 4.3 63.9 1.0 OH A:TYR216 4.5 63.2 1.0 CG A:ASP223 4.7 54.6 1.0 CZ A:TYR216 4.7 63.8 1.0 CD2 A:LEU219 4.8 54.4 1.0 CG A:LEU219 4.9 53.7 1.0 O A:HOH902 5.0 45.9 1.0

Magnesium binding site 3 out of 3 in the Mannitol-1-Phosphate Bound to the Phosphatase 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 3 of Mannitol-1-Phosphate Bound to the Phosphatase 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:Mg802 b:104.1 occ:1.00 O1 B:SO4803 2.0 132.8 1.0 OD1 B:ASP176 2.5 120.2 1.0 OE2 B:GLU175 2.7 123.0 1.0 OD2 B:ASP16 2.8 119.5 1.0 O B:ASP18 3.0 119.7 1.0 CG B:ASP176 3.4 121.2 1.0 S B:SO4803 3.4 132.8 1.0 CG B:ASP16 3.4 119.2 1.0 CA B:GLY54 3.4 134.2 1.0 OD1 B:ASP16 3.4 121.2 1.0 OG B:SER177 3.4 129.3 1.0 OD2 B:ASP176 3.6 123.0 1.0 OE1 B:GLU25 3.8 130.3 1.0 N B:GLY54 3.9 135.3 1.0 CD B:GLU175 3.9 122.2 1.0 O4 B:SO4803 3.9 132.6 1.0 CB B:SER177 4.0 130.9 1.0 O3 B:SO4803 4.2 133.4 1.0 O2 B:SO4803 4.2 132.4 1.0 N B:SER177 4.2 126.5 1.0 C B:ASP18 4.2 117.9 1.0 OE1 B:GLU175 4.6 120.8 1.0 N B:ASP176 4.7 119.8 1.0 CB B:ASP176 4.8 120.3 1.0 CD B:GLU25 4.8 130.6 1.0 CA B:SER177 4.8 130.2 1.0 CB B:ASP16 4.8 116.5 1.0 CB B:ASP18 4.8 120.6 1.0 C B:LEU53 4.8 137.8 1.0 NZ B:LYS151 4.8 127.8 1.0 C B:GLY54 4.8 137.1 1.0 CG B:GLU175 4.9 123.1 1.0 OG1 B:THR20 4.9 114.1 1.0 CA B:ASP18 4.9 117.4 1.0 CG B:GLU25 5.0 127.8 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