Magnesium in PDB 2o9j: Crystal Structure of Calcium Atpase with Bound Magnesium Fluoride and Cyclopiazonic Acid

All present enzymatic activity of Crystal Structure of Calcium Atpase with Bound Magnesium Fluoride and Cyclopiazonic Acid:
3.6.3.8;

The structure of Crystal Structure of Calcium Atpase with Bound Magnesium Fluoride and Cyclopiazonic Acid, PDB code: 2o9j was solved by H.S.Young, K.A.Moncoq, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.10 / 2.65
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	175.383, 69.875, 143.411, 90.00, 107.10, 90.00
R / Rfree (%)	24.6 / 28.7

The structure of Crystal Structure of Calcium Atpase with Bound Magnesium Fluoride and Cyclopiazonic Acid also contains other interesting chemical elements:

Fluorine	(F)	4 atoms
Sodium	(Na)	1 atom

The binding sites of Magnesium atom in the Crystal Structure of Calcium Atpase with Bound Magnesium Fluoride and Cyclopiazonic Acid (pdb code 2o9j). 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 Calcium Atpase with Bound Magnesium Fluoride and Cyclopiazonic Acid, PDB code: 2o9j:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Calcium Atpase with Bound Magnesium Fluoride and Cyclopiazonic Acid


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 Calcium Atpase with Bound Magnesium Fluoride and Cyclopiazonic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg995 b:36.8 occ:1.00 OD1 A:ASP703 1.8 49.0 1.0 O A:THR353 1.9 45.3 1.0 OD2 A:ASP351 2.0 44.5 1.0 F4 A:MF4996 2.0 35.7 1.0 O A:HOH2071 2.0 35.5 1.0 O A:HOH2061 2.2 38.6 1.0 CG A:ASP703 2.8 47.4 1.0 OD2 A:ASP703 3.1 47.9 1.0 C A:THR353 3.1 45.1 1.0 CG A:ASP351 3.1 44.5 1.0 OD1 A:ASP351 3.6 44.5 1.0 MG A:MF4996 3.8 34.0 1.0 CA A:THR353 4.0 44.8 1.0 OG1 A:THR355 4.0 45.5 1.0 OD2 A:ASP707 4.0 46.4 1.0 N A:THR353 4.1 44.8 1.0 N A:GLY354 4.1 45.2 1.0 CB A:THR353 4.2 44.6 1.0 CB A:ASP703 4.2 46.3 1.0 N A:GLY704 4.3 45.2 1.0 CA A:GLY354 4.3 45.5 1.0 CB A:ASP351 4.4 44.2 1.0 N A:ASP703 4.4 46.9 1.0 O A:GLY182 4.4 43.6 1.0 N A:THR355 4.6 46.1 1.0 CA A:ASP703 4.6 46.3 1.0 C A:ASP703 4.7 45.7 1.0 C A:GLY354 4.7 45.8 1.0 F3 A:MF4996 4.8 32.7 1.0 CG2 A:THR353 4.8 43.9 1.0 CA A:GLY182 4.8 42.6 1.0 CA A:GLY704 4.8 44.0 1.0 C A:LYS352 4.9 44.7 1.0 F1 A:MF4996 4.9 34.7 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Calcium Atpase with Bound Magnesium Fluoride and Cyclopiazonic Acid


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 Calcium Atpase with Bound Magnesium Fluoride and Cyclopiazonic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg996 b:34.0 occ:1.00 MG A:MF4996 0.0 34.0 1.0 F1 A:MF4996 2.0 34.7 1.0 F3 A:MF4996 2.0 32.7 1.0 F4 A:MF4996 2.0 35.7 1.0 F2 A:MF4996 2.0 35.4 1.0 OD1 A:ASP351 2.2 44.5 1.0 CG A:ASP351 3.2 44.5 1.0 OG1 A:THR625 3.4 40.9 1.0 O A:HOH2061 3.5 38.6 1.0 OD2 A:ASP351 3.5 44.5 1.0 N A:GLY626 3.8 40.5 1.0 N A:THR353 3.8 44.8 1.0 MG A:MG995 3.8 36.8 1.0 O A:THR181 3.8 41.5 1.0 CB A:THR353 4.0 44.6 1.0 N A:LYS352 4.2 44.3 1.0 CA A:THR625 4.2 40.7 1.0 OE1 A:GLU183 4.2 47.3 1.0 NZ A:LYS684 4.2 30.5 1.0 OG1 A:THR353 4.2 43.5 1.0 CA A:GLY182 4.3 42.6 1.0 CB A:THR625 4.3 40.5 1.0 ND2 A:ASN706 4.3 37.0 1.0 CA A:THR353 4.4 44.8 1.0 O A:THR353 4.4 45.3 1.0 O A:HOH2071 4.5 35.5 1.0 C A:THR625 4.5 40.8 1.0 O A:GLY182 4.6 43.6 1.0 C A:GLY182 4.6 43.2 1.0 CB A:ASP351 4.6 44.2 1.0 CA A:GLY626 4.7 40.6 1.0 C A:LYS352 4.7 44.7 1.0 C A:THR181 4.8 41.8 1.0 CA A:LYS352 4.8 44.5 1.0 N A:ASP627 4.9 41.1 1.0 O A:ILE624 4.9 40.9 1.0 C A:THR353 4.9 45.1 1.0 CB A:LYS352 4.9 44.0 1.0 N A:GLY182 5.0 42.4 1.0

K.Moncoq, C.A.Trieber, H.S.Young. The Molecular Basis For Cyclopiazonic Acid Inhibition of the Sarcoplasmic Reticulum Calcium Pump. J.Biol.Chem. V. 282 9748 2007.
ISSN: ISSN 0021-9258
PubMed: 17259168
DOI: 10.1074/JBC.M611653200