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Potassium in PDB 5avv: Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 8.5 Min

Protein crystallography data

The structure of Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 8.5 Min, PDB code: 5avv 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) 14.99 / 2.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 220.991, 50.841, 163.358, 90.00, 104.02, 90.00
R / Rfree (%) 27.9 / 29.3

Other elements in 5avv:

The structure of Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 8.5 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 8.5 Min (pdb code 5avv). 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 8.5 Min, PDB code: 5avv:

Potassium binding site 1 out of 1 in 5avv

Go back to Potassium Binding Sites List in 5avv
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 8.5 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 8.5 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K2005

b:82.3
occ:0.34
TL A:TL2006 0.0 82.3 0.7
O A:ALA728 2.7 68.9 1.0
O A:LYS726 2.8 70.0 1.0
OD1 A:ASP747 3.0 77.5 1.0
O A:LEU725 3.0 67.6 1.0
C A:LYS726 3.6 69.6 1.0
C A:ALA728 3.8 69.0 1.0
CG A:ASP747 3.8 76.0 1.0
OD2 A:ASP747 3.9 77.0 1.0
CA A:LYS726 4.0 69.4 1.0
N A:GLY731 4.0 67.3 1.0
C A:LEU725 4.1 68.0 1.0
N A:ALA728 4.3 69.1 1.0
O A:ASP729 4.4 69.2 1.0
C A:ASP729 4.4 68.8 1.0
CA A:ALA728 4.4 69.1 1.0
N A:LYS726 4.5 68.7 1.0
O A:ALA745 4.5 74.4 1.0
CA A:ILE730 4.5 68.2 1.0
N A:ILE730 4.5 68.4 1.0
N A:LYS727 4.6 69.3 1.0
C A:ILE730 4.6 67.8 1.0
C A:LYS727 4.6 69.2 1.0
CB A:ALA728 4.6 68.8 1.0
CA A:GLY731 4.8 67.1 1.0
N A:ASP729 4.8 69.0 1.0
O A:LYS727 5.0 69.2 1.0
CA A:ASP729 5.0 69.1 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: Mon Aug 12 12:56:10 2024

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