Magnesium in PDB 2by4: Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Boc-12ADT.

All present enzymatic activity of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Boc-12ADT.:
3.6.3.8;

The structure of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Boc-12ADT., PDB code: 2by4 was solved by A.L.Jensen, J.V.Moller, H.Soehoel, S.R.Denmeade, J.T.Isaacs, C.E.Olsen, S.B.Christensen, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 3.3
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	71.739, 71.739, 593.656, 90.00, 90.00, 90.00
R / Rfree (%)	25.4 / 31.4

The structure of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Boc-12ADT. also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Magnesium atom in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Boc-12ADT. (pdb code 2by4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Boc-12ADT., PDB code: 2by4:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Boc-12ADT.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Boc-12ADT. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1997 b:69.0 occ:0.50 OE2 A:GLU439 2.5 92.2 1.0 O2B A:ACP1996 2.6 73.0 0.5 O3A A:ACP1996 3.2 74.3 0.5 CG2 A:THR441 3.3 61.5 1.0 PB A:ACP1996 3.6 73.2 0.5 N7 A:ACP1996 3.6 69.3 0.5 O1A A:ACP1996 3.6 75.3 0.5 CD A:GLU439 3.7 88.5 1.0 NH1 A:ARG560 3.8 90.7 1.0 PA A:ACP1996 3.9 76.4 0.5 C8 A:ACP1996 4.0 69.5 0.5 NH2 A:ARG560 4.0 89.2 1.0 O5' A:ACP1996 4.1 73.6 0.5 C5 A:ACP1996 4.4 69.3 0.5 CG A:GLU439 4.4 83.9 1.0 CZ A:ARG560 4.4 87.5 1.0 O1B A:ACP1996 4.6 74.0 0.5 OE1 A:GLU439 4.6 90.2 1.0 CB A:THR441 4.6 62.6 1.0 C3B A:ACP1996 4.8 71.2 0.5 OG1 A:THR441 4.8 61.1 1.0 N6 A:ACP1996 5.0 70.0 0.5

Magnesium binding site 2 out of 2 in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Boc-12ADT.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Boc-12ADT. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1998 b:67.8 occ:1.00 OD1 A:ASP703 3.3 70.9 1.0 OD2 A:ASP707 3.6 43.2 1.0 CG A:ASP703 3.9 68.5 1.0 OD2 A:ASP703 3.9 71.3 1.0 OD1 A:ASP707 4.0 47.5 1.0 CG A:ASP707 4.2 48.2 1.0 O A:GLY182 4.7 0.5 1.0 OD1 A:ASN706 4.9 70.6 1.0 N A:ASP703 4.9 57.7 1.0

H.Soehoel, A.L.Jensen, J.V.Moller, P.Nissen, S.R.Denmeade, J.T.Isaacs, C.E.Olsen, S.B.Christensen. Natural Products As Starting Materials For Development of Second-Generation Serca Inhibitors Targeted Towards Prostate Cancer Cells Bioorg.Med.Chem. V. 14 2810 2006.
ISSN: ISSN 0968-0896
PubMed: 16412648
DOI: 10.1016/J.BMC.2005.12.001