Magnesium in PDB 4ycl: Crystal Structure of the Sr CA2+-Atpase with Bound Cpa

All present enzymatic activity of Crystal Structure of the Sr CA2+-Atpase with Bound Cpa:
3.6.3.8;

The structure of Crystal Structure of the Sr CA2+-Atpase with Bound Cpa, PDB code: 4ycl was solved by H.Ogawa, M.Takahashi, Y.Kondou, C.Toyoshima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.98 / 3.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.039, 96.029, 155.418, 90.00, 95.09, 90.00
R / Rfree (%)	19.7 / 23.7

The structure of Crystal Structure of the Sr CA2+-Atpase with Bound Cpa also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of the Sr CA2+-Atpase with Bound Cpa (pdb code 4ycl). 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 Sr CA2+-Atpase with Bound Cpa, PDB code: 4ycl:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Sr CA2+-Atpase with Bound Cpa


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 CA2+-Atpase with Bound Cpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:0.9 occ:1.00 OE1 A:GLN56 2.0 0.7 1.0 O A:HOH2003 2.1 0.3 1.0 O2 A:CZA1003 2.1 0.1 1.0 O A:HOH2001 2.2 0.0 1.0 O A:HOH2002 2.3 0.3 1.0 O1 A:CZA1003 2.6 0.9 1.0 C6 A:CZA1003 2.9 0.4 1.0 C2 A:CZA1003 3.2 0.2 1.0 CD A:GLN56 3.3 0.2 1.0 C3 A:CZA1003 3.3 0.5 1.0 NE2 A:GLN56 4.1 0.2 1.0 CB A:GLN56 4.3 0.3 1.0 CG A:GLN56 4.3 0.2 1.0 C5 A:CZA1003 4.4 0.2 1.0 CA A:GLY105 4.4 0.4 1.0 O A:ASN101 4.5 0.7 1.0 C1 A:CZA1003 4.6 0.2 1.0 C4 A:CZA1003 4.6 0.2 1.0 O A:GLN56 4.8 1.0 1.0 CA A:GLN56 4.8 0.7 1.0 CA A:ALA102 5.0 0.2 1.0

M.Takahashi, Y.Kondou, C.Toyoshima. Interdomain Communication in Calcium Pump As Revealed in the Crystal Structures with Transmembrane Inhibitors Proc.Natl.Acad.Sci.Usa V. 104 5800 2007.
ISSN: ISSN 0027-8424
PubMed: 17389383
DOI: 10.1073/PNAS.0700979104