Magnesium in PDB 7ocn: Crystal Structure of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii

The structure of Crystal Structure of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocn 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)	48.52 / 2.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.496, 157.418, 219.802, 90, 90, 90
R / Rfree (%)	23.7 / 26.7

The structure of Crystal Structure of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii also contains other interesting chemical elements:

Chlorine	(Cl)	4 atoms
Bromine	(Br)	1 atom

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

Magnesium binding site 1 out of 3 in the Crystal Structure 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 Crystal Structure of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg801 b:70.3 occ:1.00 OD2 A:ASP16 2.4 62.4 1.0 O A:ASP18 2.5 64.9 1.0 OD1 A:ASP176 2.5 68.6 1.0 CG A:ASP16 3.3 61.8 1.0 CG A:ASP176 3.4 68.9 1.0 O4 A:SO4802 3.4 118.6 1.0 OD2 A:ASP176 3.5 70.6 1.0 OD1 A:ASP16 3.5 62.8 1.0 OE2 A:GLU175 3.6 67.5 1.0 C A:ASP18 3.7 65.3 1.0 O3 A:SO4802 3.9 117.7 1.0 OG A:SER177 4.2 68.1 1.0 S A:SO4802 4.2 118.0 1.0 CB A:SER177 4.3 68.8 1.0 N A:SER177 4.6 67.1 1.0 CA A:ASP18 4.6 65.8 1.0 OE2 A:GLU25 4.6 75.1 1.0 N A:GLY19 4.6 64.9 1.0 CB A:ASP16 4.7 60.5 1.0 O1 A:SO4802 4.7 117.9 1.0 N A:ASP18 4.7 64.5 1.0 CB A:ASP18 4.7 67.7 1.0 CB A:ASP176 4.8 67.3 1.0 OG1 A:THR20 4.8 60.7 1.0 CA A:GLY19 4.8 64.6 1.0 CD A:GLU175 4.8 66.3 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure 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 Crystal Structure of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg805 b:86.1 occ:1.00 O A:HOH938 2.5 72.0 1.0 O A:HOH906 2.6 75.9 1.0 O A:THR412 2.6 74.8 1.0 OE1 A:GLN524 3.0 81.8 1.0 O A:LEU373 3.1 86.3 1.0 O A:HOH911 3.3 68.4 1.0 OD1 A:ASP411 3.3 80.2 1.0 O A:LYS375 3.4 97.5 1.0 C A:THR412 3.8 73.5 1.0 O A:HOH927 4.0 49.0 1.0 CD A:GLN524 4.2 81.9 1.0 C A:LEU373 4.3 87.2 1.0 CB A:ALA378 4.4 98.2 1.0 CG A:ASP411 4.4 79.4 1.0 N A:THR412 4.5 73.6 1.0 N A:LYS375 4.5 96.0 1.0 C A:LYS375 4.5 99.2 1.0 CG2 A:VAL413 4.6 75.6 1.0 N A:VAL413 4.7 72.9 1.0 CG A:GLN524 4.7 81.7 1.0 CA A:VAL413 4.7 74.2 1.0 CA A:THR412 4.8 72.1 1.0 OD2 A:ASP411 5.0 81.1 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure 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 3 of Crystal Structure of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg802 b:97.4 occ:1.00 OD2 B:ASP16 2.6 125.5 1.0 OD1 B:ASP176 2.6 129.0 1.0 O B:ASP18 2.7 129.7 1.0 OE2 B:GLU175 2.9 129.3 1.0 OE1 B:GLU25 3.3 140.2 1.0 CG B:ASP16 3.4 124.4 1.0 OG B:SER177 3.5 137.0 1.0 O B:HOH904 3.6 82.3 1.0 OD1 B:ASP16 3.6 124.9 1.0 CG B:ASP176 3.6 130.1 1.0 CA B:GLY54 3.6 143.5 1.0 CB B:SER177 3.8 138.7 1.0 C B:ASP18 3.9 127.8 1.0 OD2 B:ASP176 4.0 132.1 1.0 N B:GLY54 4.1 145.7 1.0 CD B:GLU175 4.1 128.6 1.0 N B:SER177 4.3 134.8 1.0 NZ B:LYS151 4.4 133.7 1.0 CD B:GLU25 4.5 140.7 1.0 CB B:ASP18 4.5 129.0 1.0 CA B:ASP18 4.6 126.2 1.0 CA B:SER177 4.7 138.6 1.0 CB B:ASP16 4.7 122.3 1.0 OE1 B:GLU175 4.8 127.0 1.0 N B:ASP176 4.8 127.9 1.0 N B:ASP18 4.8 123.6 1.0 CG B:GLU25 4.8 138.4 1.0 OG1 B:THR20 4.9 125.7 1.0 N B:GLY19 4.9 127.1 1.0 CB B:ASP176 4.9 129.1 1.0 C B:LEU53 5.0 149.0 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