Potassium 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:

Chlorine	(Cl)	2 atoms
Magnesium	(Mg)	2 atoms

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

Potassium binding site 1 out of 1 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 Potassium with other atoms in the K 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:K809 b:73.3 occ:1.00 O A:HOH906 2.8 35.2 1.0 O A:HOH907 3.1 46.4 1.0 O A:HOH916 3.6 27.6 1.0 OD2 A:ASP223 3.6 41.7 1.0 O A:HOH919 3.7 31.6 1.0 O A:HOH904 4.3 42.4 1.0 CG A:ASP223 4.4 41.0 1.0 CD2 A:LEU219 4.6 41.9 1.0 OE1 A:GLN102 4.6 43.4 1.0 CG A:LEU219 4.6 41.2 1.0 CE2 A:TYR216 4.7 46.9 1.0 OD1 A:ASP223 4.7 40.9 1.0 NH1 A:ARG106 4.8 42.8 1.0 OH A:TYR216 4.9 46.9 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