Magnesium in PDB 5svj: Crystal Structure of the Atp-Gated Human P2X3 Ion Channel in the Closed, Apo State

The structure of Crystal Structure of the Atp-Gated Human P2X3 Ion Channel in the Closed, Apo State, PDB code: 5svj was solved by S.E.Mansoor, W.Lu, W.Oosterheert, M.Shekhar, E.Tajkhorshid, E.Gouaux, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.07 / 2.98
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	120.170, 120.170, 236.580, 90.00, 90.00, 120.00
R / Rfree (%)	21.3 / 25.9

The structure of Crystal Structure of the Atp-Gated Human P2X3 Ion Channel in the Closed, Apo State also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of the Atp-Gated Human P2X3 Ion Channel in the Closed, Apo State (pdb code 5svj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Atp-Gated Human P2X3 Ion Channel in the Closed, Apo State, PDB code: 5svj:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Atp-Gated Human P2X3 Ion Channel in the Closed, Apo State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Atp-Gated Human P2X3 Ion Channel in the Closed, Apo State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:64.6 occ:1.00 OD1 A:ASP158 3.2 0.6 1.0 O A:GLU156 4.1 95.7 1.0 OE1 A:GLU109 4.1 0.7 1.0 CG A:ASP158 4.4 0.9 1.0 OE2 A:GLU109 4.5 98.8 1.0 CD A:GLU109 4.6 97.9 1.0 CB A:GLU156 4.7 90.5 1.0 C A:GLU156 4.8 88.7 1.0 OE1 A:GLU156 4.9 74.5 1.0 OD2 A:ASP158 4.9 0.0 1.0 CB A:GLU111 4.9 76.0 1.0

S.E.Mansoor, W.Lu, W.Oosterheert, M.Shekhar, E.Tajkhorshid, E.Gouaux. X-Ray Structures Define Human P2X3 Receptor Gating Cycle and Antagonist Action. Nature V. 538 66 2016.
ISSN: ESSN 1476-4687
PubMed: 27626375
DOI: 10.1038/NATURE19367