Calcium in PDB 7sxc: Ctnc-Tni Chimera Complexed with Calcium

The binding sites of Calcium atom in the Ctnc-Tni Chimera Complexed with Calcium (pdb code 7sxc). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Ctnc-Tni Chimera Complexed with Calcium, PDB code: 7sxc:

Calcium binding site 1 out of 1 in the Ctnc-Tni Chimera Complexed with Calcium


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ctnc-Tni Chimera Complexed with Calcium within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca201 b:74.5 occ:1.00 H A:THR71 2.2 72.1 1.0 OG A:SER69 2.4 44.0 1.0 H A:GLY70 2.4 30.0 1.0 OD1 A:ASP65 2.4 62.4 1.0 OD1 A:ASP67 2.5 64.2 1.0 O A:THR71 2.5 62.2 1.0 H A:SER69 2.6 24.4 1.0 HG A:SER69 2.6 42.4 1.0 N A:THR71 3.1 35.5 1.0 N A:GLY70 3.2 15.4 1.0 N A:SER69 3.3 72.2 1.0 CG A:ASP67 3.4 50.1 1.0 C A:THR71 3.5 61.4 1.0 CB A:SER69 3.5 40.2 1.0 OD2 A:ASP67 3.6 53.1 1.0 HA A:ASP65 3.6 34.2 1.0 CG A:ASP65 3.6 34.2 1.0 CA A:SER69 3.7 54.4 1.0 C A:SER69 3.8 24.0 1.0 CA A:THR71 3.9 21.1 1.0 HB2 A:SER69 4.0 5.2 1.0 C A:GLY70 4.1 11.0 1.0 CA A:GLY70 4.1 24.2 1.0 H A:GLY68 4.1 45.2 1.0 OG1 A:THR71 4.2 54.1 1.0 HG3 A:GLU76 4.2 55.2 1.0 HG1 A:THR71 4.2 24.3 1.0 HA2 A:GLY70 4.3 71.4 1.0 HB3 A:SER69 4.3 5.4 1.0 N A:GLY68 4.4 32.3 1.0 OD2 A:ASP65 4.4 32.1 1.0 H A:ASP67 4.4 71.2 1.0 C A:GLY68 4.4 24.3 1.0 HA A:VAL72 4.5 71.5 1.0 CA A:ASP65 4.6 70.3 1.0 HA2 A:GLY68 4.6 43.2 1.0 CB A:THR71 4.6 61.4 1.0 HG21 A:ILE61 4.7 73.1 1.0 OD2 A:ASP73 4.7 54.3 1.0 CB A:ASP65 4.7 75.4 1.0 N A:VAL72 4.7 23.3 1.0 CA A:GLY68 4.7 55.3 1.0 HA A:THR71 4.7 2.2 1.0 H A:GLU66 4.8 42.3 1.0 HA A:SER69 4.8 63.2 1.0 CB A:ASP67 4.8 24.3 1.0 HG23 A:ILE61 4.8 22.5 1.0 HG22 A:ILE61 4.9 2.1 1.0 C A:ASP67 4.9 33.3 1.0 O A:SER69 5.0 50.1 1.0 N A:ASP67 5.0 25.3 1.0

L.Poppe, J.J.Hartman, A.Romero, J.D.Reagan. Structural and Thermodynamic Model For the Activation of Cardiac Troponin. Biochemistry V. 61 741 2022.
ISSN: ISSN 0006-2960
PubMed: 35349258
DOI: 10.1021/ACS.BIOCHEM.2C00084