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Calcium in PDB 1top: Structure of Chicken Skeletal Muscle Troponin-C at 1.78 Angstroms Resolution

Protein crystallography data

The structure of Structure of Chicken Skeletal Muscle Troponin-C at 1.78 Angstroms Resolution, PDB code: 1top was solved by M.Sundaralingam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.78
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 66.700, 66.700, 60.800, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Chicken Skeletal Muscle Troponin-C at 1.78 Angstroms Resolution (pdb code 1top). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Chicken Skeletal Muscle Troponin-C at 1.78 Angstroms Resolution, PDB code: 1top:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1top

Go back to Calcium Binding Sites List in 1top
Calcium binding site 1 out of 2 in the Structure of Chicken Skeletal Muscle Troponin-C at 1.78 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Chicken Skeletal Muscle Troponin-C at 1.78 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca163

b:15.1
occ:1.00
O A:HOH176 1.5 31.4 1.0
OD1 A:ASN108 1.9 23.2 1.0
O A:PHE112 2.1 22.2 1.0
OD1 A:ASP106 2.2 15.5 1.0
OE1 A:GLU117 2.4 14.3 1.0
OD1 A:ASP110 2.4 18.8 1.0
OE2 A:GLU117 2.5 20.6 1.0
CD A:GLU117 2.8 18.6 1.0
CG A:ASN108 3.1 19.0 1.0
CG A:ASP110 3.3 31.2 1.0
CG A:ASP106 3.3 24.0 1.0
C A:PHE112 3.4 10.7 1.0
ND2 A:ASN108 3.7 27.6 1.0
OD2 A:ASP110 3.7 17.9 1.0
OD2 A:ASP106 4.2 15.0 1.0
CA A:ASP106 4.2 10.5 1.0
CB A:ASP106 4.2 13.6 1.0
N A:PHE112 4.2 9.5 1.0
N A:ASP110 4.3 18.7 1.0
CA A:PHE112 4.3 12.3 1.0
N A:ILE113 4.3 7.8 1.0
CG A:GLU117 4.3 21.0 1.0
CB A:ASN108 4.4 20.6 1.0
N A:ASN108 4.4 24.2 1.0
OD2 A:ASP114 4.4 16.0 1.0
CA A:ILE113 4.4 12.3 1.0
CB A:ASP110 4.4 18.8 1.0
C A:ASP106 4.4 15.0 1.0
O A:HOH166 4.6 27.3 1.0
O A:HOH187 4.6 78.7 1.0
N A:LYS107 4.6 15.8 1.0
N A:ASP114 4.6 14.7 1.0
CB A:PHE112 4.7 21.6 1.0
N A:ALA109 4.7 20.5 1.0
CA A:ASN108 4.7 23.9 1.0
CA A:ASP110 4.8 17.1 1.0
C A:ASN108 4.9 26.1 1.0
O A:ASP106 4.9 19.3 1.0
CG A:ASP114 4.9 20.3 1.0
C A:ILE113 4.9 13.7 1.0

Calcium binding site 2 out of 2 in 1top

Go back to Calcium Binding Sites List in 1top
Calcium binding site 2 out of 2 in the Structure of Chicken Skeletal Muscle Troponin-C at 1.78 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Chicken Skeletal Muscle Troponin-C at 1.78 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca164

b:13.4
occ:1.00
O A:HOH209 1.5 37.5 1.0
O A:ARG148 2.1 14.0 1.0
OD1 A:ASN144 2.1 15.6 1.0
OD1 A:ASP142 2.3 13.4 1.0
OD1 A:ASP146 2.4 12.5 1.0
OE1 A:GLU153 2.4 10.9 1.0
OE2 A:GLU153 2.6 12.9 1.0
CD A:GLU153 2.9 13.8 1.0
CG A:ASP146 3.3 22.3 1.0
CG A:ASN144 3.3 15.7 1.0
C A:ARG148 3.3 11.1 1.0
CG A:ASP142 3.4 15.6 1.0
OD2 A:ASP146 3.6 25.1 1.0
ND2 A:ASN144 4.0 16.5 1.0
CB A:ASP142 4.2 13.5 1.0
N A:ARG148 4.2 19.4 1.0
CA A:ASP142 4.2 14.8 1.0
OD2 A:ASP142 4.2 16.3 1.0
N A:ILE149 4.3 8.8 1.0
CA A:ARG148 4.3 14.0 1.0
N A:ASP146 4.4 15.0 1.0
N A:ASN144 4.4 18.5 1.0
CG A:GLU153 4.4 10.1 1.0
CA A:ILE149 4.4 14.8 1.0
CB A:ASP146 4.5 13.8 1.0
O A:HOH355 4.5 75.8 1.0
CB A:ASN144 4.6 9.7 1.0
N A:LYS143 4.6 15.9 1.0
C A:ASP142 4.6 25.6 1.0
O A:HOH210 4.6 24.9 1.0
N A:ASP150 4.6 11.9 1.0
CG A:ARG148 4.7 28.9 1.0
N A:ASN145 4.7 10.1 1.0
CA A:ASN144 4.8 12.7 1.0
CA A:ASP146 4.9 11.3 1.0
C A:ASN144 4.9 15.4 1.0

Reference:

K.A.Satyshur, D.Pyzalska, M.Greaser, S.T.Rao, M.Sundaralingam. Structure of Chicken Skeletal Muscle Troponin C at 1.78 A Resolution. Acta Crystallogr.,Sect.D V. 50 40 1994.
ISSN: ISSN 0907-4449
PubMed: 15299475
DOI: 10.1107/S090744499300798X
Page generated: Tue Jul 8 02:20:39 2025

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