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Magnesium in PDB 5avs: Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 3.5 Min

Protein crystallography data

The structure of Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 3.5 Min, PDB code: 5avs 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 (°) 221.904, 50.871, 164.190, 90.00, 104.45, 90.00
R / Rfree (%) 28.5 / 28.4

Other elements in 5avs:

The structure of Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 3.5 Min also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Potassium (K) 2 atoms
Thallium (Tl) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 3.5 Min (pdb code 5avs). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 3.5 Min, PDB code: 5avs:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5avs

Go back to Magnesium Binding Sites List in 5avs
Magnesium binding site 1 out of 2 in the Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 3.5 Min


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 3.5 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2001

b:62.4
occ:1.00
MG A:MF42001 0.0 62.4 1.0
F3 A:MF42001 2.0 63.0 1.0
F1 A:MF42001 2.0 61.8 1.0
F4 A:MF42001 2.0 59.8 1.0
F2 A:MF42001 2.0 61.0 1.0
OD2 A:ASP376 2.5 55.3 1.0
OG1 A:THR617 3.3 54.5 1.0
O A:THR219 3.5 58.2 1.0
CG A:ASP376 3.6 56.4 1.0
N A:GLY618 3.8 54.8 1.0
N A:THR378 3.8 55.0 1.0
CB A:THR378 3.8 55.3 1.0
MG A:MG2002 3.9 56.5 1.0
OE1 A:GLU221 3.9 61.4 1.0
OD1 A:ASP376 3.9 55.7 1.0
OG1 A:THR378 4.0 55.6 1.0
CA A:GLY220 4.1 57.9 1.0
CB A:THR617 4.1 54.3 1.0
CA A:THR617 4.3 54.4 1.0
N A:LYS377 4.4 55.7 1.0
O A:GLY220 4.4 58.0 1.0
CA A:THR378 4.4 55.3 1.0
C A:GLY220 4.4 58.2 1.0
ND2 A:ASN720 4.5 58.2 1.0
NZ A:LYS698 4.5 58.0 1.0
C A:THR219 4.5 58.6 1.0
N A:ASP619 4.6 56.4 1.0
C A:THR617 4.6 54.4 1.0
CA A:GLY618 4.6 55.3 1.0
O A:THR378 4.6 55.2 1.0
N A:GLY220 4.8 58.0 1.0
C A:LYS377 4.8 55.2 1.0
CB A:ASP376 4.9 56.1 1.0
CD A:GLU221 4.9 60.7 1.0
CA A:LYS377 5.0 55.2 1.0
C A:GLY618 5.0 55.9 1.0

Magnesium binding site 2 out of 2 in 5avs

Go back to Magnesium Binding Sites List in 5avs
Magnesium binding site 2 out of 2 in the Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 3.5 Min


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Kinetics By X-Ray Crystallography: Tl+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 3.5 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2002

b:56.5
occ:1.00
F2 A:MF42001 1.9 61.0 1.0
O A:THR378 1.9 55.2 1.0
OD2 A:ASP717 1.9 59.8 1.0
OD1 A:ASP376 2.0 55.7 1.0
CG A:ASP717 3.0 58.9 1.0
CG A:ASP376 3.0 56.4 1.0
C A:THR378 3.1 55.5 1.0
OD1 A:ASP717 3.3 61.6 1.0
OD2 A:ASP376 3.4 55.3 1.0
CA A:THR378 3.8 55.3 1.0
MG A:MF42001 3.9 62.4 1.0
N A:THR378 4.0 55.0 1.0
CB A:THR378 4.0 55.3 1.0
N A:GLY379 4.2 55.9 1.0
OG1 A:THR380 4.2 57.0 1.0
OD2 A:ASP721 4.2 61.1 1.0
N A:GLY718 4.2 59.5 1.0
O A:GLY220 4.3 58.0 1.0
CB A:ASP717 4.3 58.9 1.0
CB A:ASP376 4.3 56.1 1.0
N A:ASP717 4.4 58.5 1.0
CA A:GLY379 4.5 56.6 1.0
F4 A:MF42001 4.6 59.8 1.0
F1 A:MF42001 4.6 61.8 1.0
CG2 A:THR378 4.6 53.4 1.0
C A:ASP717 4.7 59.3 1.0
CA A:ASP717 4.7 59.0 1.0
CA A:GLY220 4.7 57.9 1.0
N A:THR380 4.7 57.0 1.0
C A:LYS377 4.8 55.2 1.0
CA A:GLY718 4.8 60.2 1.0
C A:GLY379 4.8 57.2 1.0
C A:GLY220 5.0 58.2 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 Sep 29 00:37:16 2024

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