Magnesium in PDB 5aw5: Kinetics By X-Ray Crystallography: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 2.2 Min

The structure of Kinetics By X-Ray Crystallography: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 2.2 Min, PDB code: 5aw5 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 / 2.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	219.497, 50.543, 162.600, 90.00, 104.10, 90.00
R / Rfree (%)	30.3 / 31.6

The structure of Kinetics By X-Ray Crystallography: Rb+-Substitution of Bound K+ in the E2.MGF42-.2K+ Crystal After 2.2 Min also contains other interesting chemical elements:

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

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 2.2 Min (pdb code 5aw5). 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 2.2 Min, PDB code: 5aw5:
Jump to Magnesium binding site number: 1; 2;

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 2.2 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 2.2 Min within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2001 b:73.5 occ:1.00 MG A:MF42001 0.0 73.5 1.0 F3 A:MF42001 2.0 74.1 1.0 F1 A:MF42001 2.0 72.9 1.0 F4 A:MF42001 2.0 70.9 1.0 F2 A:MF42001 2.0 72.2 1.0 OD1 A:ASP376 2.5 66.4 1.0 OG1 A:THR617 3.3 65.7 1.0 O A:THR219 3.5 69.4 1.0 CG A:ASP376 3.6 67.6 1.0 N A:GLY618 3.8 66.0 1.0 N A:THR378 3.8 66.1 1.0 CB A:THR378 3.8 66.5 1.0 MG A:MG2002 3.9 67.7 1.0 OE1 A:GLU221 3.9 72.5 1.0 OD2 A:ASP376 3.9 66.9 1.0 OG1 A:THR378 4.0 66.8 1.0 CA A:GLY220 4.1 69.1 1.0 CB A:THR617 4.1 65.4 1.0 CA A:THR617 4.3 65.5 1.0 N A:LYS377 4.4 66.8 1.0 O A:GLY220 4.4 69.1 1.0 CA A:THR378 4.4 66.4 1.0 C A:GLY220 4.4 69.3 1.0 ND2 A:ASN720 4.5 69.4 1.0 NZ A:LYS698 4.5 69.2 1.0 C A:THR219 4.5 69.8 1.0 N A:ASP619 4.6 67.5 1.0 C A:THR617 4.6 65.6 1.0 CA A:GLY618 4.6 66.4 1.0 O A:THR378 4.6 66.4 1.0 N A:GLY220 4.8 69.2 1.0 C A:LYS377 4.8 66.3 1.0 CB A:ASP376 4.9 67.3 1.0 CD A:GLU221 4.9 71.8 1.0 CA A:LYS377 5.0 66.4 1.0 C A:GLY618 5.0 67.0 1.0

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 2.2 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 2.2 Min within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2002 b:67.7 occ:1.00 F2 A:MF42001 1.9 72.2 1.0 O A:THR378 1.9 66.4 1.0 OD1 A:ASP717 1.9 71.0 1.0 OD2 A:ASP376 2.0 66.9 1.0 CG A:ASP717 3.0 70.1 1.0 CG A:ASP376 3.0 67.6 1.0 C A:THR378 3.1 66.7 1.0 OD2 A:ASP717 3.3 72.7 1.0 OD1 A:ASP376 3.4 66.4 1.0 CA A:THR378 3.8 66.4 1.0 MG A:MF42001 3.9 73.5 1.0 N A:THR378 4.0 66.1 1.0 CB A:THR378 4.0 66.5 1.0 N A:GLY379 4.2 67.0 1.0 OG1 A:THR380 4.2 68.1 1.0 OD2 A:ASP721 4.2 72.3 1.0 N A:GLY718 4.2 70.7 1.0 O A:GLY220 4.3 69.1 1.0 CB A:ASP717 4.3 70.0 1.0 CB A:ASP376 4.3 67.3 1.0 N A:ASP717 4.4 69.7 1.0 CA A:GLY379 4.5 67.8 1.0 F4 A:MF42001 4.6 70.9 1.0 F1 A:MF42001 4.6 72.9 1.0 CG2 A:THR378 4.6 64.5 1.0 C A:ASP717 4.7 70.5 1.0 CA A:ASP717 4.7 70.2 1.0 CA A:GLY220 4.7 69.1 1.0 N A:THR380 4.7 68.1 1.0 C A:LYS377 4.8 66.3 1.0 CA A:GLY718 4.8 71.3 1.0 C A:GLY379 4.8 68.3 1.0 C A:GLY220 5.0 69.3 1.0

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