Magnesium in PDB 1yv0: Crystal Structure of Skeletal Muscle Troponin in the CA2+-Free State

The structure of Crystal Structure of Skeletal Muscle Troponin in the CA2+-Free State, PDB code: 1yv0 was solved by M.V.Vinogradova, D.B.Stone, G.G.Malanina, C.Karatzaferi, R.Cooke, R.A.Mendelson, R.J.Fletterick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 7.00
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	134.662, 134.662, 102.070, 90.00, 90.00, 90.00
R / Rfree (%)	35.8 / 35.9

The binding sites of Magnesium atom in the Crystal Structure of Skeletal Muscle Troponin in the CA2+-Free State (pdb code 1yv0). 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 Skeletal Muscle Troponin in the CA2+-Free State, PDB code: 1yv0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Skeletal Muscle Troponin in the CA2+-Free State


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 Skeletal Muscle Troponin in the CA2+-Free State within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg162 b:35.5 occ:1.00 OD1 C:ASP109 2.1 21.7 1.0 CG C:ASP109 2.8 21.9 1.0 OD2 C:ASP113 3.0 25.1 1.0 ND2 C:ASN107 3.1 21.7 1.0 OD2 C:ASP109 3.2 19.1 1.0 OE1 C:GLU116 3.7 23.6 1.0 CG C:ASN107 3.8 22.1 1.0 OD1 C:ASN107 3.9 21.3 1.0 CB C:ASP109 4.0 22.5 1.0 CG C:ASP113 4.1 26.3 1.0 O C:PHE111 4.3 28.6 1.0 CD C:GLU116 4.4 23.8 1.0 OD1 C:ASP113 4.7 25.7 1.0 C C:PHE111 4.7 28.9 1.0 OE2 C:GLU116 4.8 24.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Skeletal Muscle Troponin in the CA2+-Free State


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 Skeletal Muscle Troponin in the CA2+-Free State within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg163 b:25.7 occ:1.00 OE1 C:GLU152 2.4 14.2 1.0 OD1 C:ASN143 2.7 24.4 1.0 OE2 C:GLU152 2.9 20.5 1.0 CD C:GLU152 3.0 20.4 1.0 OD1 C:ASP145 3.1 25.0 1.0 CG C:ASN143 3.4 24.0 1.0 N C:ASP149 3.4 25.5 1.0 ND2 C:ASN143 3.4 25.2 1.0 CG C:ASP145 3.8 25.5 1.0 CA C:ILE148 3.8 24.9 1.0 OD2 C:ASP145 3.8 26.5 1.0 O C:ARG147 3.8 26.0 1.0 OD2 C:ASP141 3.9 21.7 1.0 C C:ILE148 4.1 23.1 1.0 N C:ILE148 4.1 25.6 1.0 C C:ARG147 4.1 25.9 1.0 NE2 T:GLN243 4.2 23.4 1.0 CB C:ASP149 4.3 25.3 1.0 OD2 C:ASP149 4.4 23.9 1.0 CG C:ASP149 4.4 23.9 1.0 CG C:GLU152 4.4 21.7 1.0 CA C:ASP141 4.4 23.5 1.0 CA C:ASP149 4.4 24.2 1.0 CG C:ASP141 4.5 21.8 1.0 CB C:ASP141 4.6 22.8 1.0 CD T:GLN243 4.7 22.9 1.0 CG T:GLN243 4.8 23.9 1.0 CB C:ASN143 4.8 23.2 1.0 CB C:GLU152 4.8 23.6 1.0 OD1 C:ASP149 4.9 25.4 1.0 C C:ASP141 5.0 23.9 1.0

M.V.Vinogradova, D.B.Stone, G.G.Malanina, C.Karatzaferi, R.Cooke, R.A.Mendelson, R.J.Fletterick. CA2+-Regulated Structural Changes in Troponin Proc.Natl.Acad.Sci.Usa V. 102 5038 2005.
ISSN: ISSN 0027-8424
PubMed: 15784741
DOI: 10.1073/PNAS.0408882102