Magnesium in PDB 8b22: Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+

The structure of Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+, PDB code: 8b22 was solved by J.Strauss, K.Vidilaseris, A.Goldman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.70 / 3.98
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	83.928, 110.626, 106.154, 90, 108.26, 90
R / Rfree (%)	23.3 / 26.5

The binding sites of Magnesium atom in the Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+ (pdb code 8b22). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+, PDB code: 8b22:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg802 b:125.4 occ:1.00 O A:HOH901 2.7 133.3 1.0 O3 A:DPO801 2.7 214.3 1.0 OD1 A:ASP465 3.1 194.8 1.0 MG A:MG804 3.1 144.5 1.0 CG A:ASP465 4.1 173.7 1.0 P1 A:DPO801 4.2 214.3 1.0 OD1 A:ASP218 4.3 197.7 1.0 OD2 A:ASP465 4.4 164.1 1.0 O A:ASP465 4.7 193.3 1.0 O4 A:DPO801 4.8 214.3 1.0 ND2 A:ASN229 4.8 179.3 1.0 OE1 A:GLU217 4.9 182.2 1.0 O1 A:DPO801 4.9 214.3 1.0

Magnesium binding site 2 out of 4 in the Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg803 b:193.8 occ:1.00 OD2 A:ASP202 2.4 160.1 1.0 O2 A:DPO801 2.5 214.3 1.0 OD2 A:ASP692 2.6 173.5 1.0 O1 A:DPO801 2.8 214.3 1.0 P1 A:DPO801 3.1 214.3 1.0 CG A:ASP202 3.4 161.2 1.0 CG A:ASP692 3.4 146.8 1.0 OD1 A:ASP692 3.5 146.2 1.0 OD1 A:ASP202 3.7 191.9 1.0 O4 A:DPO801 3.7 214.3 1.0 O5 A:DPO801 3.8 214.3 1.0 NZ A:LYS199 4.2 129.4 1.0 P2 A:DPO801 4.3 214.3 1.0 O3 A:DPO801 4.5 214.3 1.0 CB A:ASP202 4.7 146.6 1.0 OD2 A:ASP688 4.8 176.9 1.0 CB A:ASP692 4.8 123.2 1.0 O7 A:DPO801 4.8 214.3 1.0

Magnesium binding site 3 out of 4 in the Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg804 b:144.5 occ:1.00 OE1 A:GLU217 2.7 182.2 1.0 O3 A:DPO801 3.0 214.3 1.0 MG A:MG802 3.1 125.4 1.0 OE2 A:GLU217 3.1 169.2 1.0 CD A:GLU217 3.2 180.5 1.0 O A:HOH901 3.2 133.3 1.0 OD2 A:ASP228 3.4 182.6 1.0 O1 A:DPO801 3.4 214.3 1.0 OD1 A:ASP218 3.7 197.7 1.0 P1 A:DPO801 3.8 214.3 1.0 CG A:ASP228 4.2 181.2 1.0 ND2 A:ASN229 4.5 179.3 1.0 CG A:GLU217 4.6 178.8 1.0 CB A:ASP228 4.6 166.3 1.0 O2 A:DPO801 4.9 214.3 1.0 CG A:ASP218 4.9 205.7 1.0 O4 A:DPO801 4.9 214.3 1.0 OD1 A:ASP202 5.0 191.9 1.0

Magnesium binding site 4 out of 4 in the Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Time-Resolved Structure of K+-Dependent Na+-Ppase From Thermotoga Maritima 300-Seconds Post Reaction Initiation with Na+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg805 b:145.3 occ:1.00 O5 A:DPO801 2.5 214.3 1.0 O7 A:DPO801 2.6 214.3 1.0 P2 A:DPO801 2.9 214.3 1.0 OD2 A:ASP696 3.1 138.3 1.0 CE A:LYS695 3.1 136.9 1.0 NZ A:LYS695 3.3 160.3 1.0 O6 A:DPO801 3.6 214.3 1.0 OD1 A:ASP696 3.7 133.7 1.0 CG A:ASP696 3.8 140.1 1.0 CD A:LYS695 4.4 134.9 1.0 O4 A:DPO801 4.4 214.3 1.0 OD1 A:ASP692 4.6 146.2 1.0 NZ A:LYS199 4.8 129.4 1.0 CG A:LYS695 5.0 125.6 1.0

J.Strauss, K.Vidilaseris, A.Goldman. The Structure of Tmppase After 300 Second Soaking with Sodium Ion To Be Published.