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

The structure of Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii, PDB code: 7ocp 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)	48.59 / 2.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.661, 157.692, 219.289, 90, 90, 90
R / Rfree (%)	22 / 25.5

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

Magnesium

(Mg)

2 atoms

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

Chlorine binding site 1 out of 2 in the Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld 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 Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl806 b:73.5 occ:1.00 N A:GLY99 3.1 59.6 1.0 NE2 A:GLN102 3.2 55.9 1.0 N A:GLN244 3.2 59.4 1.0 CA A:GLY99 3.5 58.3 1.0 CB A:ASN243 3.7 58.4 1.0 CB A:GLN244 3.8 60.2 1.0 CG A:GLN244 3.9 60.1 1.0 CG A:GLN102 3.9 55.1 1.0 CA A:ASN243 3.9 58.9 1.0 CD A:GLN102 4.0 55.1 1.0 C A:ASN243 4.1 59.8 1.0 CA A:GLN244 4.1 60.1 1.0 C A:LYS98 4.1 61.1 1.0 CE1 A:TYR216 4.2 62.2 1.0 CG A:LYS98 4.3 64.8 1.0 C A:GLY99 4.4 57.7 1.0 CA A:LYS98 4.4 62.5 1.0 CD A:GLN244 4.4 60.6 1.0 NE2 A:GLN244 4.6 60.4 1.0 N A:LEU100 4.8 57.5 1.0 CG A:ASN243 4.8 59.0 1.0 N A:LEU245 4.8 59.0 1.0 C A:GLN244 4.8 60.0 1.0 CD1 A:TYR216 4.9 61.8 1.0 CB A:GLN102 4.9 54.5 1.0 CB A:LYS98 4.9 63.9 1.0

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


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1005 b:97.0 occ:1.00 NE2 B:GLN102 3.1 95.6 1.0 N B:GLY99 3.1 101.5 1.0 N B:GLN244 3.3 94.3 1.0 CA B:GLY99 3.6 100.4 1.0 CG B:GLN102 3.7 93.2 1.0 CB B:ASN243 3.8 91.1 1.0 CG B:GLN244 3.8 98.8 1.0 CA B:ASN243 3.9 91.4 1.0 CB B:GLN244 3.9 98.2 1.0 CD B:GLN102 3.9 93.9 1.0 C B:ASN243 4.1 92.6 1.0 C B:GLY99 4.1 99.6 1.0 C B:LYS98 4.2 104.0 1.0 CA B:GLN244 4.2 95.6 1.0 CD B:GLN244 4.3 101.5 1.0 NE2 B:GLN244 4.4 102.0 1.0 CA B:LYS98 4.4 105.0 1.0 CG B:LYS98 4.4 104.7 1.0 N B:LEU100 4.5 100.3 1.0 O B:GLY99 4.6 98.1 1.0 CB B:GLN102 4.7 93.5 1.0 N B:GLN102 4.7 93.4 1.0 CE2 B:TYR216 4.8 102.7 1.0 N B:VAL101 4.8 96.3 1.0 CB B:VAL101 5.0 93.2 1.0 CG B:ASN243 5.0 89.7 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