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Potassium in PDB 1kf6: E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno

Enzymatic activity of E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno

All present enzymatic activity of E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno:
1.3.99.1;

Protein crystallography data

The structure of E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno, PDB code: 1kf6 was solved by T.M.Iverson, C.Luna-Chavez, L.R.Croal, G.Cecchini, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 96.505, 137.836, 273.451, 90.00, 90.00, 90.00
R / Rfree (%) 23.1 / 28

Other elements in 1kf6:

The structure of E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno also contains other interesting chemical elements:

Iron (Fe) 18 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno (pdb code 1kf6). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno, PDB code: 1kf6:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1kf6

Go back to Potassium Binding Sites List in 1kf6
Potassium binding site 1 out of 2 in the E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K720

b:49.9
occ:1.00
O A:GLY359 2.7 26.9 1.0
O A:THR357 2.7 28.6 1.0
O A:SER381 2.8 23.7 1.0
O A:MET358 2.8 29.2 1.0
O A:GLU379 2.9 27.7 1.0
C A:MET358 3.2 28.6 1.0
C A:GLY359 3.5 24.0 1.0
C A:THR357 3.7 26.1 1.0
C A:GLU379 3.8 28.9 1.0
CA A:MET358 3.9 24.4 1.0
C A:SER381 3.9 29.4 1.0
N A:GLY359 3.9 29.2 1.0
OH A:TYR356 4.2 31.8 1.0
CA A:GLU379 4.2 26.4 1.0
CA A:GLY359 4.2 25.1 1.0
N A:SER381 4.2 27.1 1.0
N A:MET358 4.2 24.6 1.0
N A:GLY360 4.3 19.9 1.0
CG A:GLU379 4.3 27.1 1.0
CA A:GLY360 4.4 18.3 1.0
O A:GLY378 4.5 18.8 1.0
CA A:SER381 4.6 29.4 1.0
CG2 A:THR357 4.6 34.2 1.0
CZ A:TYR356 4.6 27.3 1.0
C A:CYS380 4.7 26.5 1.0
CB A:THR357 4.7 30.3 1.0
CE2 A:TYR356 4.7 23.4 1.0
N A:CYS380 4.8 25.3 1.0
CA A:THR357 4.9 26.7 1.0
N A:SER382 4.9 35.6 1.0
CB A:GLU379 5.0 23.7 1.0

Potassium binding site 2 out of 2 in 1kf6

Go back to Potassium Binding Sites List in 1kf6
Potassium binding site 2 out of 2 in the E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of E. Coli Quinol-Fumarate Reductase with Bound Inhibitor Hqno within 5.0Å range:
probe atom residue distance (Å) B Occ
M:K820

b:80.2
occ:1.00
O M:THR357 2.7 70.2 1.0
O M:GLU379 2.8 65.5 1.0
O M:GLY359 2.8 81.8 1.0
O M:MET358 3.0 72.8 1.0
O M:SER381 3.2 68.1 1.0
C M:MET358 3.3 74.1 1.0
C M:GLU379 3.6 62.4 1.0
CA M:MET358 3.7 73.0 1.0
C M:GLY359 3.7 80.2 1.0
C M:THR357 3.8 70.4 1.0
N M:GLY359 3.9 75.2 1.0
CA M:GLU379 4.0 64.8 1.0
C M:SER381 4.1 66.1 1.0
N M:MET358 4.2 71.4 1.0
N M:GLY360 4.4 80.8 1.0
O M:GLY378 4.4 61.0 1.0
CA M:GLY359 4.4 78.1 1.0
N M:SER381 4.4 57.9 1.0
CG M:GLU379 4.5 66.1 1.0
CA M:GLY360 4.5 80.0 1.0
N M:CYS380 4.6 57.0 1.0
OH M:TYR356 4.6 77.5 1.0
C M:CYS380 4.6 54.6 1.0
CG2 M:THR357 4.7 69.5 1.0
CA M:SER381 4.8 61.9 1.0
CB M:GLU379 4.8 66.6 1.0
N M:SER382 4.8 68.4 1.0
CE1 M:TYR356 4.8 77.5 1.0
CA M:CYS380 4.9 54.6 1.0
CA M:SER382 5.0 67.7 1.0
CD2 M:HIS386 5.0 85.4 1.0
CZ M:TYR356 5.0 77.7 1.0
O M:CYS380 5.0 49.4 1.0

Reference:

T.M.Iverson, C.Luna-Chavez, L.R.Croal, G.Cecchini, D.C.Rees. Crystallographic Studies of the Escherichia Coli Quinol-Fumarate Reductase with Inhibitors Bound to the Quinol-Binding Site. J.Biol.Chem. V. 277 16124 2002.
ISSN: ISSN 0021-9258
PubMed: 11850430
DOI: 10.1074/JBC.M200815200
Page generated: Sun Dec 13 22:47:35 2020

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