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Calcium in PDB 5tnc: Refined Crystal Structure of Troponin C From Turkey Skeletal Muscle at 2.0 Angstroms Resolution

Protein crystallography data

The structure of Refined Crystal Structure of Troponin C From Turkey Skeletal Muscle at 2.0 Angstroms Resolution, PDB code: 5tnc was solved by O.Herzberg, M.N.G.James, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 66.550, 66.550, 60.910, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Refined Crystal Structure of Troponin C From Turkey Skeletal Muscle at 2.0 Angstroms Resolution (pdb code 5tnc). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Refined Crystal Structure of Troponin C From Turkey Skeletal Muscle at 2.0 Angstroms Resolution, PDB code: 5tnc:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 5tnc

Go back to Calcium Binding Sites List in 5tnc
Calcium binding site 1 out of 2 in the Refined Crystal Structure of Troponin C From Turkey Skeletal Muscle at 2.0 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Refined Crystal Structure of Troponin C From Turkey Skeletal Muscle at 2.0 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca163

b:8.1
occ:1.00
O A:PHE112 2.1 7.3 1.0
OE1 A:GLU117 2.2 10.8 1.0
OD1 A:ASP110 2.3 10.9 1.0
O A:HOH173 2.3 14.3 1.0
OD2 A:ASP106 2.4 9.7 1.0
OD1 A:ASN108 2.4 12.3 1.0
OE2 A:GLU117 2.6 11.8 1.0
CD A:GLU117 2.7 11.6 1.0
CG A:ASP110 3.1 13.3 1.0
C A:PHE112 3.4 7.9 1.0
CG A:ASN108 3.4 14.1 1.0
CG A:ASP106 3.5 8.1 1.0
OD2 A:ASP110 3.6 12.7 1.0
ND2 A:ASN108 4.0 12.7 1.0
N A:PHE112 4.1 9.1 1.0
OD1 A:ASP106 4.1 7.3 1.0
CG A:GLU117 4.2 12.4 1.0
N A:ASP110 4.2 15.3 1.0
CA A:ASP106 4.2 9.3 1.0
CA A:PHE112 4.2 7.5 1.0
N A:ASN108 4.3 14.8 1.0
N A:ILE113 4.3 6.6 1.0
CB A:ASP110 4.4 13.5 1.0
CB A:ASP106 4.4 9.3 1.0
CA A:ILE113 4.4 8.4 1.0
N A:ASP114 4.5 6.7 1.0
OD2 A:ASP114 4.5 10.5 1.0
C A:ASP106 4.5 10.8 1.0
CB A:PHE112 4.6 8.0 1.0
CB A:ASN108 4.6 14.8 1.0
N A:LYS107 4.6 12.2 1.0
N A:ALA109 4.7 15.3 1.0
CG A:ASP114 4.7 10.9 1.0
CA A:ASP110 4.8 12.3 1.0
CA A:ASN108 4.8 15.1 1.0
N A:GLY111 4.9 11.1 1.0
C A:ILE113 4.9 8.2 1.0
C A:ASN108 4.9 16.0 1.0
O A:HOH238 5.0 20.2 0.7

Calcium binding site 2 out of 2 in 5tnc

Go back to Calcium Binding Sites List in 5tnc
Calcium binding site 2 out of 2 in the Refined Crystal Structure of Troponin C From Turkey Skeletal Muscle at 2.0 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Refined Crystal Structure of Troponin C From Turkey Skeletal Muscle at 2.0 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca164

b:8.9
occ:1.00
OD1 A:ASN144 2.3 5.3 1.0
OE2 A:GLU153 2.4 6.9 1.0
OD2 A:ASP142 2.4 14.8 1.0
O A:ARG148 2.4 10.6 1.0
OE1 A:GLU153 2.5 10.2 1.0
OD1 A:ASP146 2.5 10.2 1.0
O A:HOH167 2.7 11.9 1.0
CD A:GLU153 2.8 9.7 1.0
CG A:ASN144 3.4 8.2 1.0
CG A:ASP146 3.4 12.8 1.0
CG A:ASP142 3.5 16.0 1.0
C A:ARG148 3.6 12.2 1.0
OD2 A:ASP146 3.9 17.0 1.0
ND2 A:ASN144 4.0 10.9 1.0
N A:ASN144 4.1 11.5 1.0
N A:ASP146 4.2 14.8 1.0
CB A:ASP142 4.2 15.2 1.0
CG A:GLU153 4.3 7.6 1.0
CA A:ASP142 4.3 13.4 1.0
OD1 A:ASP142 4.3 15.9 1.0
N A:ARG148 4.3 14.2 1.0
N A:LYS143 4.5 13.9 1.0
C A:ASP142 4.5 14.8 1.0
N A:ILE149 4.5 10.9 1.0
CA A:ILE149 4.5 10.8 1.0
CA A:ARG148 4.6 14.3 1.0
CB A:ASN144 4.6 10.6 1.0
CB A:ASP146 4.6 13.1 1.0
CA A:ASN144 4.7 10.3 1.0
N A:ASN145 4.7 10.6 1.0
N A:ASP150 4.7 9.2 1.0
CA A:ASP146 4.7 14.7 1.0
CG A:ARG148 4.8 24.9 1.0
OD2 A:ASP150 4.8 15.4 1.0
N A:GLY147 4.8 14.3 1.0
C A:ASN144 4.8 10.1 1.0
C A:ASP146 5.0 14.5 1.0

Reference:

O.Herzberg, M.N.James. Refined Crystal Structure of Troponin C From Turkey Skeletal Muscle at 2.0 A Resolution. J.Mol.Biol. V. 203 761 1988.
ISSN: ISSN 0022-2836
PubMed: 3210231
DOI: 10.1016/0022-2836(88)90208-2
Page generated: Wed Jul 9 10:21:42 2025

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