Sodium in PDB 7ocs: Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii

The structure of Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii, PDB code: 7ocs 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)	48.61 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	88.888, 212.626, 98.819, 90, 112.81, 90
R / Rfree (%)	21.5 / 24.7

The structure of Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii also contains other interesting chemical elements:

Chlorine	(Cl)	10 atoms
Magnesium	(Mg)	1 atom

The binding sites of Sodium atom in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii (pdb code 7ocs). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii, PDB code: 7ocs:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ B:Na813 b:39.6 occ:1.00 O B:HOH1088 2.4 49.6 1.0 OD2 B:ASP223 2.5 43.2 1.0 O B:HOH932 2.8 30.6 1.0 NH1 B:ARG106 3.1 34.1 1.0 CG B:ASP223 3.4 39.8 1.0 OD1 B:ASP223 3.6 40.1 1.0 O B:HOH939 3.7 43.0 1.0 O B:HOH997 4.0 25.3 1.0 CZ B:ARG106 4.0 35.0 1.0 CG B:LYS510 4.2 36.1 1.0 OD2 B:ASP268 4.2 34.0 1.0 O B:HOH961 4.2 42.5 1.0 O B:HOH950 4.2 23.6 1.0 OE1 B:GLN102 4.4 33.0 1.0 O B:HOH901 4.4 34.3 1.0 CB B:LYS510 4.5 32.3 1.0 CG B:LEU219 4.5 31.0 1.0 NE B:ARG106 4.6 33.9 1.0 CD2 B:LEU219 4.6 30.9 1.0 CD1 B:LEU219 4.6 31.1 1.0 NH2 B:ARG106 4.8 34.6 1.0 CB B:ASP223 4.8 34.2 1.0

Sodium binding site 2 out of 2 in the Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Mannitol-1-Phosphate Bound to the Phosphatase Domain of the Bifunctional Mannitol-1-Phosphate Dehydrogenase/Phosphatase Mtld-D16A From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ C:Na808 b:60.6 occ:1.00 OD2 C:ASP268 2.9 43.1 1.0 O C:HOH922 2.9 38.3 1.0 O C:HOH967 3.1 54.3 1.0 NH1 C:ARG106 3.3 50.5 1.0 CB C:LYS510 3.7 52.7 1.0 O C:HOH921 3.8 68.9 1.0 CG C:ASP268 4.0 40.7 1.0 O C:HOH952 4.1 65.5 1.0 OD2 C:ASP223 4.1 67.2 1.0 CG C:LYS510 4.1 57.3 1.0 OE1 C:GLN102 4.2 47.1 1.0 CB C:ASP268 4.3 37.5 1.0 CZ C:ARG106 4.5 50.6 1.0 O C:HOH911 4.5 34.2 1.0 NE1 C:TRP267 4.8 39.7 1.0 CD1 C:LEU507 4.8 58.2 1.0 NH2 C:ARG106 5.0 50.5 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