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Calcium in PDB 1npq: Structure of A Rhodamine-Labeled N-Domain Troponin C Mutant (CA2+ Saturated) in Complex with Skeletal Troponin I 115- 131

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of A Rhodamine-Labeled N-Domain Troponin C Mutant (CA2+ Saturated) in Complex with Skeletal Troponin I 115- 131 (pdb code 1npq). 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 A Rhodamine-Labeled N-Domain Troponin C Mutant (CA2+ Saturated) in Complex with Skeletal Troponin I 115- 131, PDB code: 1npq:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1npq

Go back to Calcium Binding Sites List in 1npq
Calcium binding site 1 out of 2 in the Structure of A Rhodamine-Labeled N-Domain Troponin C Mutant (CA2+ Saturated) in Complex with Skeletal Troponin I 115- 131


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of A Rhodamine-Labeled N-Domain Troponin C Mutant (CA2+ Saturated) in Complex with Skeletal Troponin I 115- 131 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca132

b:0.6
occ:1.00
HG A:SER70 2.4 1.1 1.0
OD2 A:ASP66 2.5 0.8 1.0
OE2 A:GLU77 2.8 1.2 1.0
O A:THR72 2.9 0.6 1.0
OD1 A:ASP68 3.0 0.7 1.0
OE1 A:GLU77 3.0 1.2 1.0
OG A:SER70 3.0 0.6 1.0
HA A:ASP66 3.1 0.6 1.0
CD A:GLU77 3.3 0.5 1.0
CG A:ASP66 3.3 0.6 1.0
HB3 A:ASP66 3.7 0.6 1.0
HG1 A:THR72 3.8 1.1 1.0
CB A:ASP66 3.8 0.5 1.0
CG A:ASP68 3.9 0.9 1.0
H A:THR72 3.9 0.6 1.0
CA A:ASP66 3.9 0.5 1.0
OD2 A:ASP68 4.0 1.0 1.0
C A:THR72 4.1 0.5 1.0
H A:SER70 4.2 0.7 1.0
OD1 A:ASP66 4.2 0.8 1.0
OG1 A:THR72 4.2 0.7 1.0
CB A:SER70 4.3 0.6 1.0
H A:ASP68 4.3 1.2 1.0
H A:GLU67 4.3 1.1 1.0
HA A:ILE73 4.3 0.4 1.0
HB2 A:SER70 4.4 0.7 1.0
H A:ASP74 4.4 0.5 1.0
HB2 A:ASP74 4.6 0.9 1.0
N A:THR72 4.6 0.6 1.0
H A:GLY71 4.7 0.6 1.0
H A:GLY69 4.7 0.9 1.0
CG A:GLU77 4.8 0.4 1.0
C A:ASP66 4.8 0.7 1.0
CA A:THR72 4.8 0.6 1.0
N A:GLU67 4.9 0.8 1.0
HB2 A:ASP66 4.9 0.5 1.0
HB3 A:SER70 4.9 0.7 1.0
N A:SER70 4.9 0.7 1.0
N A:ASP66 4.9 0.5 1.0

Calcium binding site 2 out of 2 in 1npq

Go back to Calcium Binding Sites List in 1npq
Calcium binding site 2 out of 2 in the Structure of A Rhodamine-Labeled N-Domain Troponin C Mutant (CA2+ Saturated) in Complex with Skeletal Troponin I 115- 131


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of A Rhodamine-Labeled N-Domain Troponin C Mutant (CA2+ Saturated) in Complex with Skeletal Troponin I 115- 131 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca133

b:0.8
occ:1.00
HA A:ASP30 2.1 0.7 1.0
OE2 A:GLU41 2.2 1.4 1.0
H A:ALA31 2.4 1.0 1.0
OD1 A:ASP30 2.6 0.8 1.0
O A:ASP36 2.8 0.7 1.0
CD A:GLU41 2.8 0.8 1.0
OD1 A:ASP32 2.8 0.9 1.0
OE1 A:GLU41 2.8 1.5 1.0
CA A:ASP30 3.0 0.7 1.0
N A:ALA31 3.2 0.8 1.0
HB3 A:ASP30 3.2 0.9 1.0
CB A:ASP30 3.3 0.8 1.0
CG A:ASP30 3.4 0.8 1.0
H A:ASP32 3.4 0.9 1.0
H A:ASP36 3.5 1.4 1.0
H A:GLY33 3.5 0.9 1.0
C A:ASP30 3.5 0.8 1.0
C A:ASP36 3.6 0.6 1.0
N A:ASP36 3.9 0.8 1.0
HA A:ILE37 4.0 0.5 1.0
CG A:ASP32 4.0 1.1 1.0
HB3 A:ALA31 4.1 1.3 1.0
N A:ASP30 4.1 0.7 1.0
N A:ASP32 4.2 1.0 1.0
H A:GLY35 4.2 1.2 1.0
CG A:GLU41 4.3 0.6 1.0
CA A:ASP36 4.3 0.7 1.0
H A:GLY34 4.3 1.3 1.0
CA A:ALA31 4.4 0.9 1.0
HA A:ASP36 4.4 0.7 1.0
HB2 A:ASP30 4.4 0.9 1.0
O A:PHE29 4.4 0.7 1.0
N A:GLY33 4.4 1.0 1.0
HG2 A:GLU41 4.5 0.7 1.0
HG12 A:ILE37 4.5 0.6 1.0
N A:ILE37 4.6 0.5 1.0
OD2 A:ASP30 4.6 0.9 1.0
HG3 A:GLU41 4.7 0.9 1.0
C A:PHE29 4.7 0.7 1.0
O A:ASP30 4.7 1.1 1.0
OD2 A:ASP32 4.7 1.2 1.0
C A:ALA31 4.7 1.0 1.0
H A:ASP30 4.8 0.7 1.0
HA3 A:GLY35 4.8 1.3 1.0
C A:GLY35 4.8 1.2 1.0
HA2 A:GLY33 4.8 1.4 1.0
CB A:ALA31 4.8 0.8 1.0
CA A:ILE37 4.8 0.5 1.0
N A:GLY35 4.9 1.2 1.0

Reference:

P.Mercier, R.E.Ferguson, M.Irving, J.E.T.Corrie, D.R.Trentham, B.D.Sykes. uc(Nmr) Structure of A Bifunctional Rhodamine Labeled N-Domain of Troponin C Complexed with the Regulatory "Switch" Peptide From Troponin I: Implications For in Situ Fluorescence Studies in Muscle Fibers Biochemistry V. 42 4333 2003.
ISSN: ISSN 0006-2960
PubMed: 12693929
DOI: 10.1021/BI027041N
Page generated: Thu Jul 11 12:58:33 2024

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