Strontium in PDB 5hxs: Structural Mechanisms of Extracellular Ion Exchange and Induced Binding-Site Occlusion in the Sodium-Calcium Exchanger NCX_MJ Soaked with 2.5 Mm Na+ and 10MM SR2+

The structure of Structural Mechanisms of Extracellular Ion Exchange and Induced Binding-Site Occlusion in the Sodium-Calcium Exchanger NCX_MJ Soaked with 2.5 Mm Na+ and 10MM SR2+, PDB code: 5hxs was solved by J.Liao, Y.X.Jiang, J.D.Faraldo-Gomez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.79
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.516, 72.353, 96.000, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 27.4

The binding sites of Strontium atom in the Structural Mechanisms of Extracellular Ion Exchange and Induced Binding-Site Occlusion in the Sodium-Calcium Exchanger NCX_MJ Soaked with 2.5 Mm Na+ and 10MM SR2+ (pdb code 5hxs). This binding sites where shown within 5.0 Angstroms radius around Strontium atom.
In total 2 binding sites of Strontium where determined in the Structural Mechanisms of Extracellular Ion Exchange and Induced Binding-Site Occlusion in the Sodium-Calcium Exchanger NCX_MJ Soaked with 2.5 Mm Na+ and 10MM SR2+, PDB code: 5hxs:
Jump to Strontium binding site number: 1; 2;

Strontium binding site 1 out of 2 in the Structural Mechanisms of Extracellular Ion Exchange and Induced Binding-Site Occlusion in the Sodium-Calcium Exchanger NCX_MJ Soaked with 2.5 Mm Na+ and 10MM SR2+


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 1 of Structural Mechanisms of Extracellular Ion Exchange and Induced Binding-Site Occlusion in the Sodium-Calcium Exchanger NCX_MJ Soaked with 2.5 Mm Na+ and 10MM SR2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Sr401 b:55.0 occ:0.68 OE1 A:GLU213 2.4 51.6 1.0 OE2 A:GLU213 2.4 66.1 1.0 OE1 A:GLU54 2.4 53.2 1.0 OE2 A:GLU54 2.4 72.3 1.0 O A:THR50 2.4 60.1 1.0 O A:THR209 2.5 66.1 1.0 CD A:GLU213 2.7 52.0 1.0 CD A:GLU54 2.7 62.1 1.0 C A:THR50 3.6 51.9 1.0 C A:THR209 3.7 62.7 1.0 CA A:SER51 3.9 55.6 1.0 CG A:GLU213 4.2 46.6 1.0 N A:SER51 4.2 56.1 1.0 CG A:GLU54 4.2 57.6 1.0 OG A:SER51 4.3 54.3 1.0 CA A:SER210 4.3 61.6 1.0 N A:SER210 4.5 65.9 1.0 OD1 A:ASP240 4.6 58.1 1.0 CB A:SER51 4.7 54.3 1.0 CA A:THR209 4.7 63.3 1.0 CA A:THR50 4.8 48.9 1.0 CB A:THR209 4.8 61.7 1.0 C A:SER51 4.8 52.6 1.0 CB A:THR50 4.9 51.2 1.0 CB A:GLU213 4.9 45.2 1.0 CB A:GLU54 5.0 57.8 1.0 CD A:PRO53 5.0 55.5 1.0

Strontium binding site 2 out of 2 in the Structural Mechanisms of Extracellular Ion Exchange and Induced Binding-Site Occlusion in the Sodium-Calcium Exchanger NCX_MJ Soaked with 2.5 Mm Na+ and 10MM SR2+


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 2 of Structural Mechanisms of Extracellular Ion Exchange and Induced Binding-Site Occlusion in the Sodium-Calcium Exchanger NCX_MJ Soaked with 2.5 Mm Na+ and 10MM SR2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Sr402 b:71.6 occ:1.00 OD1 A:ASP121 2.4 68.2 1.0 OD2 A:ASP127 2.4 58.0 1.0 O A:ILE118 2.4 61.2 1.0 O A:GLY122 2.7 65.8 1.0 O A:HOH509 3.0 54.0 1.0 CG A:ASP121 3.1 73.5 1.0 OD2 A:ASP121 3.2 82.5 1.0 CG A:ASP127 3.5 52.7 1.0 C24 A:OLC411 3.6 73.0 1.0 C A:ILE118 3.6 60.9 1.0 C A:GLY122 3.7 60.6 1.0 O23 A:OLC411 3.8 79.3 1.0 OD1 A:ASP127 3.9 56.1 1.0 C22 A:OLC411 4.1 75.3 1.0 C21 A:OLC411 4.3 84.4 1.0 N A:SER124 4.3 56.5 1.0 O25 A:OLC411 4.3 79.8 1.0 O A:HOH502 4.3 52.5 1.0 CA A:PHE123 4.4 52.5 1.0 CB A:ASP121 4.4 58.6 1.0 N A:GLY122 4.4 56.3 1.0 N A:PHE123 4.4 58.3 1.0 CA A:ILE118 4.5 60.4 1.0 N A:GLY119 4.6 59.4 1.0 CA A:GLY119 4.6 56.9 1.0 C A:ASP121 4.6 64.2 1.0 OG A:SER124 4.7 57.0 1.0 CA A:GLY122 4.7 60.1 1.0 CB A:ILE118 4.7 55.6 1.0 CB A:ASP127 4.8 51.1 1.0 C A:PHE123 4.8 57.0 1.0 CA A:ASP121 4.9 67.7 1.0 N A:ASP121 4.9 71.0 1.0 CB A:SER124 5.0 58.0 1.0

J.Liao, F.Marinelli, C.Lee, Y.Huang, J.D.Faraldo-Gomez, Y.Jiang. Mechanism of Extracellular Ion Exchange and Binding-Site Occlusion in A Sodium/Calcium Exchanger Nat.Struct.Mol.Biol. V. 23 590 2016.
ISSN: ESSN 1545-9985
PubMed: 27183196
DOI: 10.1038/NSMB.3230