Chlorine 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:

Magnesium

(Mg)

3 atoms

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was 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:

Chlorine binding site 1 out of 1 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 Chlorine with other atoms in the Cl 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:Cl805 b:67.3 occ:1.00 N A:GLY99 3.0 57.5 1.0 N A:GLN244 3.3 60.2 1.0 NE2 A:GLN102 3.3 54.8 1.0 CA A:GLY99 3.4 56.0 1.0 CB A:ASN243 3.7 58.2 1.0 CG A:GLN244 3.7 61.9 1.0 CG A:GLN102 3.8 53.7 1.0 CA A:ASN243 3.8 58.7 1.0 CB A:GLN244 3.9 62.0 1.0 C A:GLY99 4.0 54.6 1.0 C A:ASN243 4.0 60.0 1.0 CD A:GLN102 4.1 53.9 1.0 C A:LYS98 4.2 59.1 1.0 CA A:GLN244 4.2 61.7 1.0 CD A:GLN244 4.2 62.2 1.0 N A:LEU100 4.4 54.7 1.0 CA A:LYS98 4.5 61.3 1.0 NE2 A:GLN244 4.5 62.1 1.0 O A:GLY99 4.6 53.6 1.0 CB A:GLN102 4.7 52.9 1.0 N A:GLN102 4.7 53.0 1.0 CG A:LYS98 4.8 63.5 1.0 N A:VAL101 4.8 54.0 1.0 OE1 A:GLN244 4.9 63.5 1.0 CE1 A:TYR216 4.9 63.5 1.0 CG A:ASN243 4.9 58.8 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