Potassium in PDB 7aqa: Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A

Enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A

All present enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A:
1.7.2.4;

Protein crystallography data

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A, PDB code: 7aqa 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) 62.67 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 68.824, 76.834, 108.513, 90, 93.47, 90
R / Rfree (%) 15.6 / 19.4

Other elements in 7aqa:

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Sodium (Na) 1 atom
Copper (Cu) 11 atoms
Chlorine (Cl) 3 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A (pdb code 7aqa). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A, PDB code: 7aqa:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 7aqa

Go back to Potassium Binding Sites List in 7aqa
Potassium binding site 1 out of 2 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A


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, H382A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K705

b:21.2
occ:0.48
OE1 A:GLU469 2.4 18.6 0.5
O A:HOH830 2.5 37.3 1.0
O B:HOH827 2.5 29.0 1.0
O B:HOH828 2.6 29.5 1.0
O A:HOH816 2.6 26.2 1.0
O A:LYS454 2.7 27.5 1.0
OE2 A:GLU469 2.7 24.2 0.5
CD A:GLU469 2.9 24.9 0.5
C A:LYS454 3.8 25.1 1.0
OD1 B:ASP580 4.3 46.9 1.0
O A:HIS467 4.3 23.7 1.0
CD1 B:TRP620 4.4 35.7 1.0
CG A:GLU469 4.4 25.0 0.5
CA A:LYS454 4.4 22.5 1.0
O B:HOH847 4.4 33.7 1.0
CG A:GLU492 4.6 38.9 1.0
O A:PRO468 4.7 26.6 1.0
O B:HOH958 4.7 26.6 1.0
NE1 B:TRP620 4.7 36.5 1.0
N A:GLU469 4.7 22.5 1.0
CA A:GLU469 4.8 19.2 0.5
CB A:LYS454 4.8 25.5 1.0
OE2 A:GLU492 4.8 24.8 1.0
CA A:GLU469 4.8 18.8 0.5
C A:PRO468 4.8 25.0 1.0
O B:PHE621 4.9 33.5 1.0
N A:PHE455 4.9 26.0 1.0
CB A:GLU469 5.0 18.8 0.5
CD1 A:PHE455 5.0 31.1 1.0

Potassium binding site 2 out of 2 in 7aqa

Go back to Potassium Binding Sites List in 7aqa
Potassium binding site 2 out of 2 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H382A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K705

b:18.0
occ:0.54
OE1 B:GLU469 2.5 15.4 0.5
O A:HOH849 2.5 31.1 1.0
O B:LYS454 2.5 28.7 1.0
O B:HOH816 2.6 33.4 1.0
O A:HOH828 2.6 26.2 1.0
O B:HOH916 2.6 28.8 1.0
OE2 B:GLU469 2.8 20.8 0.5
CD B:GLU469 3.0 24.5 0.5
C B:LYS454 3.7 24.9 1.0
OD1 A:ASP580 4.1 28.8 1.0
CD1 A:TRP620 4.3 32.7 1.0
CA B:LYS454 4.4 22.9 1.0
CG B:GLU469 4.5 24.8 0.5
O B:HIS467 4.5 25.5 1.0
O A:HOH968 4.5 24.8 1.0
N B:PHE455 4.7 22.3 1.0
OE1 B:GLU492 4.7 22.3 1.0
O A:HOH872 4.7 26.9 1.0
O A:PHE621 4.7 22.2 1.0
O B:PRO468 4.7 32.5 1.0
CD1 B:PHE455 4.7 30.1 1.0
CB B:LYS454 4.8 23.9 1.0
NE1 A:TRP620 4.8 37.9 1.0
CA B:PHE455 4.9 28.7 1.0
CA B:GLU469 5.0 24.8 0.5
CG B:GLU492 5.0 29.2 1.0

Reference:

L.Zhang, E.Bill, P.M.H.Kroneck, O.Einsle. A [3CU:2S] Cluster Provides Insight Into the Assembly and Function of the Cuz Site of Nitrous Oxide Reductase Chem Sci 2021.
ISSN: ESSN 2041-6539
DOI: 10.1039/D0SC05204C
Page generated: Wed Mar 3 14:20:37 2021

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy