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Magnesium in PDB 5aw6: Kinetics By X-Ray Crystallography: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 5.5 Min

Protein crystallography data

The structure of Kinetics By X-Ray Crystallography: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 5.5 Min, PDB code: 5aw6 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 / 2.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 220.606, 50.591, 163.163, 90.00, 104.60, 90.00
R / Rfree (%) 28 / 27.1

Other elements in 5aw6:

The structure of Kinetics By X-Ray Crystallography: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 5.5 Min also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Rubidium (Rb) 3 atoms
Potassium (K) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Kinetics By X-Ray Crystallography: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 5.5 Min (pdb code 5aw6). 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: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 5.5 Min, PDB code: 5aw6:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5aw6

Go back to Magnesium Binding Sites List in 5aw6
Magnesium binding site 1 out of 2 in the Kinetics By X-Ray Crystallography: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 5.5 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: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 5.5 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2001

b:66.8
occ:1.00
MG A:MF42001 0.0 66.8 1.0
F3 A:MF42001 2.0 67.4 1.0
F1 A:MF42001 2.0 66.2 1.0
F4 A:MF42001 2.0 64.2 1.0
F2 A:MF42001 2.0 65.5 1.0
OD1 A:ASP376 2.5 59.7 1.0
OG1 A:THR617 3.3 59.0 1.0
O A:THR219 3.5 62.7 1.0
CG A:ASP376 3.6 60.8 1.0
N A:GLY618 3.8 59.2 1.0
N A:THR378 3.8 59.4 1.0
CB A:THR378 3.8 59.8 1.0
MG A:MG2002 3.9 60.9 1.0
OE1 A:GLU221 3.9 65.8 1.0
OD2 A:ASP376 3.9 60.2 1.0
OG1 A:THR378 4.0 60.1 1.0
CA A:GLY220 4.1 62.4 1.0
CB A:THR617 4.1 58.7 1.0
CA A:THR617 4.3 58.8 1.0
N A:LYS377 4.4 60.1 1.0
O A:GLY220 4.4 62.4 1.0
CA A:THR378 4.4 59.7 1.0
C A:GLY220 4.4 62.6 1.0
ND2 A:ASN720 4.5 62.7 1.0
NZ A:LYS698 4.5 62.5 1.0
C A:THR219 4.5 63.1 1.0
N A:ASP619 4.6 60.8 1.0
C A:THR617 4.6 58.9 1.0
CA A:GLY618 4.6 59.7 1.0
O A:THR378 4.6 59.6 1.0
N A:GLY220 4.8 62.5 1.0
C A:LYS377 4.8 59.6 1.0
CB A:ASP376 4.9 60.5 1.0
CD A:GLU221 4.9 65.1 1.0
CA A:LYS377 5.0 59.6 1.0
C A:GLY618 5.0 60.3 1.0

Magnesium binding site 2 out of 2 in 5aw6

Go back to Magnesium Binding Sites List in 5aw6
Magnesium binding site 2 out of 2 in the Kinetics By X-Ray Crystallography: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 5.5 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: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 5.5 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2002

b:60.9
occ:1.00
F2 A:MF42001 1.9 65.5 1.0
O A:THR378 1.9 59.6 1.0
OD1 A:ASP717 1.9 64.2 1.0
OD2 A:ASP376 2.0 60.2 1.0
CG A:ASP717 3.0 63.4 1.0
CG A:ASP376 3.0 60.8 1.0
C A:THR378 3.1 60.0 1.0
OD2 A:ASP717 3.3 66.0 1.0
OD1 A:ASP376 3.4 59.7 1.0
CA A:THR378 3.8 59.7 1.0
MG A:MF42001 3.9 66.8 1.0
N A:THR378 4.0 59.4 1.0
CB A:THR378 4.0 59.8 1.0
N A:GLY379 4.2 60.3 1.0
OG1 A:THR380 4.2 61.4 1.0
OD2 A:ASP721 4.2 65.6 1.0
N A:GLY718 4.2 64.0 1.0
O A:GLY220 4.3 62.4 1.0
CB A:ASP717 4.3 63.3 1.0
CB A:ASP376 4.3 60.5 1.0
N A:ASP717 4.4 63.0 1.0
CA A:GLY379 4.5 61.0 1.0
F4 A:MF42001 4.6 64.2 1.0
F1 A:MF42001 4.6 66.2 1.0
CG2 A:THR378 4.6 57.8 1.0
C A:ASP717 4.7 63.7 1.0
CA A:ASP717 4.7 63.5 1.0
CA A:GLY220 4.7 62.4 1.0
N A:THR380 4.7 61.4 1.0
C A:LYS377 4.8 59.6 1.0
CA A:GLY718 4.8 64.6 1.0
C A:GLY379 4.8 61.6 1.0
C A:GLY220 5.0 62.6 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 00:56:56 2024

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