Magnesium in PDB 5a3q: Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp

All present enzymatic activity of Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp:
3.6.3.8;

The structure of Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp, PDB code: 5a3q was solved by J.D.Clausen, M.Bublitz, B.Arnou, C.Olesen, J.P.Andersen, J.V.Moller, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	73.80 / 3.05
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.427, 118.781, 141.828, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 25.8

The structure of Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp also contains other interesting chemical elements:

Potassium	(K)	1 atom
Vanadium	(V)	1 atom
Chlorine	(Cl)	1 atom

The binding sites of Magnesium atom in the Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp (pdb code 5a3q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp, PDB code: 5a3q:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp


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 (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1003 b:36.6 occ:1.00 O A:HOH2002 2.0 42.1 1.0 OD1 A:ASP703 2.0 73.9 1.0 O A:HOH2003 2.1 42.3 1.0 OD2 A:ASP351 2.1 54.4 1.0 O A:THR353 2.1 64.7 1.0 O2 A:VN41001 2.3 73.8 1.0 CG A:ASP703 2.9 66.2 1.0 OD2 A:ASP703 3.1 65.8 1.0 CG A:ASP351 3.1 53.9 1.0 C A:THR353 3.3 63.0 1.0 OD1 A:ASP351 3.6 61.4 1.0 V A:VN41001 3.6 57.7 1.0 O A:GLY182 3.8 59.1 1.0 OD2 A:ASP707 4.0 64.4 1.0 CA A:THR353 4.2 54.0 1.0 N A:GLY354 4.3 66.2 1.0 CB A:ASP703 4.3 59.6 1.0 CA A:GLY354 4.3 65.5 1.0 CB A:ASP351 4.3 56.8 1.0 CB A:THR353 4.4 56.4 1.0 OG1 A:THR355 4.4 50.4 1.0 N A:GLY704 4.4 46.8 1.0 N A:THR353 4.4 56.1 1.0 CA A:GLY182 4.5 58.0 1.0 N A:ASP703 4.5 51.2 1.0 O1 A:VN41001 4.5 63.0 1.0 N A:THR355 4.6 55.5 1.0 C A:GLY182 4.6 50.6 1.0 O3 A:VN41001 4.6 52.7 1.0 C A:ASP703 4.7 48.8 1.0 C A:GLY354 4.7 63.9 1.0 CA A:ASP703 4.7 48.6 1.0 CG2 A:THR353 4.8 52.3 1.0 CA A:GLY704 4.8 72.2 1.0 OD1 A:ASN706 4.9 40.3 1.0 O A:HOH2001 5.0 89.0 1.0 CG A:ASP707 5.0 61.7 1.0 C A:LYS352 5.0 50.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the (Sr) Calcium Atpase E2-Vanadate Complex Bound to Thapsigargin and Tnp-Amppcp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1004 b:0.4 occ:1.00 O A:HOH2004 1.7 84.2 1.0 O1G A:DL51002 1.8 0.3 1.0 OD1 A:ASN628 2.2 95.2 1.0 O2B A:DL51002 2.6 0.0 1.0 PG A:DL51002 3.3 0.7 1.0 CG A:ASN628 3.3 57.1 1.0 PB A:DL51002 3.8 0.7 1.0 ND2 A:ASN628 3.9 54.8 1.0 O A:HOH2007 3.9 85.5 1.0 C01 A:DL51002 4.0 0.7 1.0 O3G A:DL51002 4.0 0.6 1.0 N7 A:DL51002 4.2 95.3 1.0 O2G A:DL51002 4.3 0.6 1.0 O1B A:DL51002 4.4 0.8 1.0 NH1 A:ARG560 4.4 0.6 1.0 CB A:ASN628 4.5 38.6 1.0 NH1 A:ARG678 4.7 85.0 1.0 C8 A:DL51002 5.0 94.8 1.0

J.D.Clausen, M.Bublitz, B.Arnou, C.Olesen, J.P.Andersen, J.D.Clausen, M.Bublitz, B.Arnou, C.Olesen, J.P.Andersen, J.V.Moller, P.Nissen. Crystal Structure of the Vanadate-Inhibited Ca(2+)-Atpase. Structure V. 24 617 2016.
ISSN: ISSN 0969-2126
PubMed: 27050689
DOI: 10.1016/J.STR.2016.02.018