Potassium in PDB 5avw: Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 16.5 Min

Protein crystallography data

The structure of Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 16.5 Min, PDB code: 5avw was solved by H.Ogawa, F.Cornelius, A.Hirata, C.Toyoshima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.98 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 222.476, 50.881, 163.810, 90.00, 104.67, 90.00
R / Rfree (%) 26.5 / 25.7

Other elements in 5avw:

The structure of Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 16.5 Min also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Magnesium (Mg) 2 atoms
Thallium (Tl) 3 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 16.5 Min (pdb code 5avw). 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 Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 16.5 Min, PDB code: 5avw:

Potassium binding site 1 out of 1 in 5avw

Go back to Potassium Binding Sites List in 5avw
Potassium binding site 1 out of 1 in the Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 16.5 Min


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 16.5 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K2005

b:66.2
occ:0.19
TL A:TL2006 0.0 66.2 0.8
O A:ALA728 2.7 52.9 1.0
O A:LYS726 2.8 53.9 1.0
OD1 A:ASP747 3.0 61.5 1.0
O A:LEU725 3.0 51.5 1.0
C A:LYS726 3.6 53.5 1.0
C A:ALA728 3.8 52.9 1.0
CG A:ASP747 3.8 59.9 1.0
OD2 A:ASP747 3.9 60.9 1.0
CA A:LYS726 4.0 53.3 1.0
N A:GLY731 4.0 51.2 1.0
C A:LEU725 4.1 51.9 1.0
N A:ALA728 4.3 53.0 1.0
O A:ASP729 4.4 53.1 1.0
C A:ASP729 4.4 52.8 1.0
CA A:ALA728 4.4 53.1 1.0
N A:LYS726 4.5 52.6 1.0
O A:ALA745 4.5 58.3 1.0
CA A:ILE730 4.5 52.1 1.0
N A:ILE730 4.5 52.3 1.0
N A:LYS727 4.6 53.2 1.0
C A:LYS727 4.6 53.2 1.0
C A:ILE730 4.6 51.7 1.0
CB A:ALA728 4.6 52.8 1.0
CA A:GLY731 4.8 51.0 1.0
N A:ASP729 4.8 52.9 1.0
O A:LYS727 5.0 53.2 1.0
CA A:ASP729 5.0 53.0 1.0

Reference:

H.Ogawa, F.Cornelius, A.Hirata, C.Toyoshima. Sequential Substitution of K(+) Bound to Na(+),K(+)-Atpase Visualized By X-Ray Crystallography. Nat Commun V. 6 8004 2015.
ISSN: ESSN 2041-1723
PubMed: 26258479
DOI: 10.1038/NCOMMS9004
Page generated: Sun Dec 13 23:54:21 2020

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