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

The structure of Nadph Bound to the Dehydrogenase Domain of the Bifunctional Mannitol- 1-Phosphate Dehydrogenase/Phosphatase Mtld-N374A From Acinetobacter Baumannii, PDB code: 7oct 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)	48.43 / 2.85
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.304, 156.957, 220.028, 90, 90, 90
R / Rfree (%)	22.7 / 27.8

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

Potassium	(K)	1 atom
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-N374A From Acinetobacter Baumannii (pdb code 7oct). 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-N374A From Acinetobacter Baumannii, PDB code: 7oct:
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-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 Nadph Bound to the Dehydrogenase 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:Cl808 b:64.1 occ:1.00 O A:HOH928 3.0 44.3 1.0 N A:GLN244 3.1 49.9 1.0 N A:GLY99 3.1 47.1 1.0 CA A:GLY99 3.4 45.9 1.0 NE2 A:GLN102 3.5 44.7 1.0 CB A:GLN244 3.6 51.2 1.0 CG A:GLN244 3.6 50.9 1.0 CB A:ASN243 3.7 47.8 1.0 CA A:ASN243 3.8 48.5 1.0 C A:ASN243 3.9 49.9 1.0 CA A:GLN244 3.9 51.1 1.0 CG A:GLN102 4.0 43.9 1.0 CD A:GLN244 4.1 51.0 1.0 C A:LYS98 4.2 48.1 1.0 NE2 A:GLN244 4.2 50.2 1.0 C A:GLY99 4.2 45.1 1.0 CD A:GLN102 4.2 43.9 1.0 CA A:LYS98 4.5 49.8 1.0 CE1 A:TYR216 4.6 46.8 1.0 N A:LEU100 4.6 45.3 1.0 CG A:LYS98 4.7 51.0 1.0 C A:GLN244 4.8 51.5 1.0 OE1 A:GLN244 4.8 52.0 1.0 CG A:ASN243 4.8 48.2 1.0 N A:LEU245 4.8 50.8 1.0 CB A:GLN102 5.0 43.2 1.0 O A:GLY99 5.0 44.4 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-N374A 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-N374A From Acinetobacter Baumannii within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1211 b:55.6 occ:1.00 NE B:ARG431 3.3 74.3 1.0 O B:HOH1318 3.4 46.1 1.0 NH1 B:ARG431 3.4 72.1 1.0 CG B:ARG428 3.6 67.3 1.0 CZ B:ARG431 3.8 73.7 1.0 CB B:ARG428 3.8 67.1 1.0 CA B:ARG428 3.9 68.4 1.0 CD2 B:TYR427 4.2 75.2 1.0 CE2 B:TYR427 4.2 77.3 1.0 CD B:ARG431 4.4 76.2 1.0 O B:HOH1323 4.5 49.0 1.0 N B:ARG428 4.5 68.9 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