Magnesium in PDB 4h1w: E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin

All present enzymatic activity of E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin:
3.6.3.8;

The structure of E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin, PDB code: 4h1w was solved by M.Bublitz, A.-M.L.Winther, J.Karlsen, J.V.Moller, J.B.Hansen, M.J.Buch-Pedersen, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.01 / 3.10
Space group	P 21 2 21
Cell size a, b, c (Å), α, β, γ (°)	85.870, 139.540, 141.560, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 24.7

The structure of E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Magnesium atom in the E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin (pdb code 4h1w). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin, PDB code: 4h1w:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:84.8 occ:1.00 O A:HOH1103 2.1 0.8 1.0 O A:HOH1102 2.1 0.1 1.0 O A:HOH1104 2.1 0.5 1.0 O3G A:ACP1005 2.2 0.7 1.0 PG A:ACP1005 3.6 0.5 1.0 O A:THR353 4.1 59.3 1.0 O2G A:ACP1005 4.1 0.2 1.0 OD1 A:ASP703 4.3 86.0 1.0 CB A:THR353 4.3 76.0 1.0 O1G A:ACP1005 4.3 80.8 1.0 OD2 A:ASP703 4.6 70.8 1.0 CB A:ASP351 4.6 68.5 1.0 OD1 A:ASP351 4.7 78.5 1.0 C3B A:ACP1005 4.7 41.7 1.0 CG A:ASP351 4.7 75.7 1.0 CG A:ASP703 4.8 73.1 1.0 O2B A:ACP1005 4.9 0.7 1.0 O1B A:ACP1005 4.9 0.3 1.0 C A:THR353 4.9 57.5 1.0 CA A:THR353 5.0 57.5 1.0 OG1 A:THR353 5.0 68.9 1.0

Magnesium binding site 2 out of 3 in the E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1003 b:0.8 occ:1.00 O A:HOH1105 2.1 0.5 1.0 OE1 A:GLU309 2.1 0.0 1.0 O A:VAL304 2.3 0.1 1.0 O A:ALA305 3.1 0.3 1.0 C A:ALA305 3.1 0.6 1.0 CA A:ALA305 3.2 0.8 1.0 CD A:GLU309 3.3 0.9 1.0 C A:VAL304 3.4 0.5 1.0 N A:ALA305 3.7 0.7 1.0 N A:ALA306 3.9 0.2 1.0 OE2 A:GLU309 4.0 0.4 1.0 ND2 A:ASN796 4.0 0.2 1.0 O A:ILE307 4.0 0.5 1.0 CG A:GLU309 4.4 0.1 1.0 CB A:ALA305 4.6 0.2 1.0 OD1 A:ASN796 4.6 0.9 1.0 CG A:ASN796 4.6 0.1 1.0 CA A:ALA306 4.7 0.3 1.0 CA A:VAL304 4.7 0.3 1.0 N A:ILE307 4.8 0.2 1.0 CG1 A:VAL304 4.9 0.8 1.0 O A:HOH1106 4.9 0.9 1.0 C A:ALA306 5.0 0.4 1.0 C A:ILE307 5.0 0.7 1.0

Magnesium binding site 3 out of 3 in the E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of E1 Structure of the (Sr) CA2+-Atpase in Complex with Sarcolipin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1004 b:0.1 occ:1.00 O A:HOH1106 2.0 0.9 1.0 O A:HOH1107 2.1 0.4 1.0 OD1 A:ASP800 2.2 0.3 1.0 OD1 A:ASN796 2.3 0.9 1.0 OD2 A:ASP800 2.3 0.7 1.0 CG A:ASP800 2.5 0.2 1.0 CG A:ASN796 3.3 0.1 1.0 OE2 A:GLU309 3.3 0.4 1.0 ND2 A:ASN796 3.8 0.2 1.0 O A:ASN796 3.9 0.5 1.0 CB A:ASP800 4.0 0.5 1.0 CD A:GLU309 4.2 0.9 1.0 OG1 A:THR799 4.2 0.6 1.0 OD1 A:ASN768 4.4 0.7 1.0 CB A:ASN796 4.5 0.9 1.0 OE1 A:GLU309 4.5 0.0 1.0 CA A:ASN796 4.6 0.1 1.0 C A:ASN796 4.7 0.0 1.0 O A:ALA305 4.7 0.3 1.0 N A:ASP800 4.8 0.2 1.0 CA A:ASP800 4.8 0.3 1.0

A.M.Winther, M.Bublitz, J.L.Karlsen, J.V.Moller, J.B.Hansen, P.Nissen, M.J.Buch-Pedersen. The Sarcolipin-Bound Calcium Pump Stabilizes Calcium Sites Exposed to the Cytoplasm. Nature V. 495 265 2013.
ISSN: ISSN 0028-0836
PubMed: 23455424
DOI: 10.1038/NATURE11900