Potassium in PDB 7aq3: Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D

All present enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D:
1.7.2.4;

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D, PDB code: 7aq3 was solved by L.Zhang, E.Bill, P.M.H.Kroneck, O.Einsle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.33 / 1.64
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	69.664, 76.608, 109.087, 90, 93.26, 90
R / Rfree (%)	15.6 / 19.9

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Zinc	(Zn)	2 atoms
Chlorine	(Cl)	2 atoms
Copper	(Cu)	8 atoms
Sodium	(Na)	2 atoms

The binding sites of Potassium atom in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D (pdb code 7aq3). 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 Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D, PDB code: 7aq3:

Potassium binding site 1 out of 1 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583D within 5.0Å range: probe atom residue distance (Å) B Occ B:K1905 b:20.4 occ:0.48 OE1 B:GLU469 2.4 40.6 1.0 O A:HOH899 2.5 33.2 1.0 O B:LYS454 2.5 35.7 1.0 O B:HOH2203 2.6 37.3 1.0 O B:HOH2017 2.6 35.5 1.0 O A:HOH826 2.6 36.1 1.0 OE2 B:GLU469 2.8 53.4 1.0 CD B:GLU469 2.9 52.0 1.0 C B:LYS454 3.7 30.1 1.0 OD1 A:ASP580 4.2 40.2 1.0 CA B:LYS454 4.4 32.2 1.0 CD1 A:TRP620 4.4 40.6 1.0 O A:HOH1048 4.4 29.4 1.0 O B:HIS467 4.4 26.7 1.0 CG B:GLU469 4.5 45.0 1.0 O B:PRO468 4.6 30.0 1.0 CG B:GLU492 4.7 37.2 1.0 N B:PHE455 4.7 28.9 1.0 OE1 B:GLU492 4.7 31.2 1.0 CB B:LYS454 4.8 32.7 1.0 CD1 B:PHE455 4.8 35.1 1.0 O A:PHE621 4.8 32.1 1.0 O A:HOH940 4.8 30.4 1.0 NE1 A:TRP620 4.9 36.1 1.0 C B:PRO468 4.9 29.0 1.0 CA B:GLU469 4.9 28.3 1.0 N B:GLU469 4.9 26.0 1.0 CA B:PHE455 4.9 30.2 1.0

L.Zhang, E.Bill, P.M.H.Kroneck, O.Einsle. Histidine-Gated Proton-Coupled Electron Transfer to the Cu A Site of Nitrous Oxide Reductase. J.Am.Chem.Soc. 2020.
ISSN: ESSN 1520-5126
PubMed: 33377777
DOI: 10.1021/JACS.0C10057