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Potassium in PDB 7aq5: Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583N

Enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583N

All present enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583N:
1.7.2.4;

Protein crystallography data

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583N, PDB code: 7aq5 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) 62.65 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 69.289, 76.452, 109.485, 90, 93.38, 90
R / Rfree (%) 16.1 / 19.9

Other elements in 7aq5:

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583N also contains other interesting chemical elements:

Zinc (Zn) 2 atoms
Chlorine (Cl) 3 atoms
Copper (Cu) 8 atoms
Sodium (Na) 2 atoms
Calcium (Ca) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583N (pdb code 7aq5). 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, H583N, PDB code: 7aq5:

Potassium binding site 1 out of 1 in 7aq5

Go back to Potassium Binding Sites List in 7aq5
Potassium binding site 1 out of 1 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H583N


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, H583N within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K704

b:26.4
occ:0.43
O A:HOH981 2.4 44.8 1.0
OE2 B:GLU469 2.5 61.5 1.0
O B:LYS454 2.5 37.2 1.0
O B:HOH816 2.6 41.4 1.0
O A:HOH850 2.6 38.0 1.0
O B:HOH975 2.6 48.6 1.0
OE1 B:GLU469 2.9 68.4 1.0
CD B:GLU469 3.0 68.5 1.0
C B:LYS454 3.7 31.0 1.0
CD1 A:TRP620 4.2 47.2 1.0
OD1 A:ASP580 4.3 62.6 1.0
NE1 A:TRP620 4.3 50.9 1.0
CA B:LYS454 4.4 37.1 1.0
O B:HIS467 4.4 32.0 1.0
O A:HOH1003 4.5 39.7 1.0
CG B:GLU469 4.5 58.5 1.0
OE1 B:GLU492 4.6 56.9 1.0
O B:PRO468 4.7 38.5 1.0
CB B:LYS454 4.7 35.3 1.0
N B:PHE455 4.7 31.8 1.0
O A:HOH987 4.7 38.2 1.0
O A:PHE621 4.8 39.9 1.0
CD1 B:PHE455 4.9 41.6 1.0
N B:GLU469 4.9 29.6 1.0
CA B:GLU469 4.9 33.5 1.0
CA B:PHE455 5.0 31.7 1.0
C B:PRO468 5.0 34.7 1.0

Reference:

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
Page generated: Mon Aug 12 18:41:14 2024

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