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Calcium in PDB 4qnh: Calcium-Calmodulin (T79D) Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel SK2-A

Protein crystallography data

The structure of Calcium-Calmodulin (T79D) Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel SK2-A, PDB code: 4qnh was solved by M.Zhang, J.M.Pascal, D.E.Logothetis, J.F.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.65 / 2.02
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.160, 65.960, 64.680, 90.00, 93.56, 90.00
R / Rfree (%) 18.2 / 23.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Calcium-Calmodulin (T79D) Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel SK2-A (pdb code 4qnh). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Calcium-Calmodulin (T79D) Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel SK2-A, PDB code: 4qnh:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 4qnh

Go back to Calcium Binding Sites List in 4qnh
Calcium binding site 1 out of 2 in the Calcium-Calmodulin (T79D) Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel SK2-A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Calcium-Calmodulin (T79D) Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel SK2-A within 5.0Å range:
probe atom residue distance (Å) B Occ
R:Ca1001

b:48.2
occ:1.00
O R:THR26 2.1 40.6 1.0
OD1 R:ASP20 2.3 51.8 1.0
OD1 R:ASP24 2.3 45.8 1.0
OD1 R:ASP22 2.3 62.2 1.0
O R:HOH1103 2.3 53.8 1.0
OE1 R:GLU31 2.5 35.2 1.0
OE2 R:GLU31 2.6 42.8 1.0
CD R:GLU31 2.9 44.1 1.0
HG23 R:THR26 3.1 51.6 1.0
CG R:ASP22 3.3 63.2 1.0
C R:THR26 3.3 45.9 1.0
CG R:ASP24 3.3 49.9 1.0
H R:THR26 3.4 53.0 1.0
CG R:ASP20 3.4 46.9 1.0
H R:ASP24 3.4 69.4 1.0
HA R:ASP20 3.5 51.9 1.0
H R:ASP22 3.6 76.8 1.0
OD2 R:ASP22 3.6 67.9 1.0
HG21 R:THR26 3.7 51.6 1.0
HA R:ILE27 3.7 43.5 1.0
CG2 R:THR26 3.8 43.0 1.0
OD2 R:ASP24 3.8 48.2 1.0
H R:GLY23 3.9 84.3 1.0
N R:THR26 4.1 44.2 1.0
N R:ASP24 4.1 56.9 1.0
HG23 R:THR28 4.2 47.3 1.0
CA R:ASP20 4.2 42.6 1.0
CA R:THR26 4.2 45.9 1.0
OD2 R:ASP20 4.2 46.4 1.0
H R:THR28 4.3 42.9 1.0
N R:ILE27 4.3 38.2 1.0
CB R:ASP20 4.3 42.0 1.0
CG R:GLU31 4.4 36.1 1.0
N R:GLY23 4.4 70.1 1.0
C R:ASP20 4.4 55.5 1.0
H R:LYS21 4.4 71.9 1.0
N R:ASP22 4.4 64.7 1.0
CA R:ILE27 4.4 36.3 1.0
CB R:ASP24 4.5 50.9 1.0
HG22 R:THR26 4.5 51.6 1.0
HB2 R:ASP20 4.6 51.1 1.0
CB R:ASP22 4.6 63.8 1.0
N R:LYS21 4.6 60.4 1.0
CB R:THR26 4.6 53.1 1.0
HB3 R:ASP24 4.6 61.1 1.0
HG3 R:GLU31 4.6 44.9 1.0
H R:GLY25 4.7 62.3 1.0
CA R:ASP24 4.7 51.2 1.0
CA R:ASP22 4.8 68.1 1.0
HG2 R:GLU31 4.8 44.9 1.0
HB3 R:ASP22 4.9 75.7 1.0
C R:ASP22 4.9 67.9 1.0
O R:ASP20 4.9 61.5 1.0
N R:GLY25 4.9 51.3 1.0
N R:THR28 4.9 35.8 1.0
O R:HOH1129 5.0 53.4 1.0
C R:ASP24 5.0 51.8 1.0
HB R:THR26 5.0 66.1 1.0
HB2 R:GLU31 5.0 39.7 1.0

Calcium binding site 2 out of 2 in 4qnh

Go back to Calcium Binding Sites List in 4qnh
Calcium binding site 2 out of 2 in the Calcium-Calmodulin (T79D) Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel SK2-A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Calcium-Calmodulin (T79D) Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel SK2-A within 5.0Å range:
probe atom residue distance (Å) B Occ
R:Ca1002

b:44.2
occ:1.00
O R:HOH1219 1.9 49.5 1.0
OD1 R:ASP56 2.0 40.5 1.0
OD1 R:ASP58 2.4 65.5 1.0
OE2 R:GLU67 2.4 59.8 1.0
OD1 R:ASN60 2.4 50.2 1.0
OE1 R:GLU67 2.4 51.1 1.0
O R:THR62 2.5 35.4 1.0
CD R:GLU67 2.8 52.6 1.0
CG R:ASP56 3.1 49.8 1.0
CG R:ASP58 3.2 63.1 1.0
OD2 R:ASP58 3.3 68.6 1.0
CG R:ASN60 3.3 46.7 1.0
HD22 R:ASN60 3.4 61.7 1.0
H R:ASN60 3.5 56.2 1.0
H R:THR62 3.6 54.6 1.0
C R:THR62 3.7 44.7 1.0
HA R:ASP56 3.7 71.8 1.0
ND2 R:ASN60 3.7 50.6 1.0
HA R:ILE63 3.7 43.9 1.0
OD2 R:ASP56 3.8 45.4 1.0
H R:ASP64 3.9 49.6 1.0
H R:ASP58 3.9 91.1 1.0
H R:GLY59 4.1 69.6 1.0
CB R:ASP56 4.2 50.4 1.0
CG R:GLU67 4.3 51.5 1.0
N R:ASN60 4.3 46.1 1.0
N R:THR62 4.3 44.5 1.0
CA R:ASP56 4.3 59.0 1.0
HB2 R:ASP56 4.3 61.5 1.0
OD2 R:ASP64 4.4 54.3 1.0
OG1 R:THR62 4.4 37.2 1.0
H R:ALA57 4.5 71.0 1.0
CA R:ILE63 4.5 35.4 1.0
N R:GLY59 4.5 57.4 1.0
N R:ASP64 4.5 41.2 1.0
N R:ILE63 4.5 35.5 1.0
HD21 R:ASN60 4.5 61.7 1.0
N R:ASP58 4.6 76.5 1.0
H R:GLY61 4.6 49.4 1.0
CB R:ASP58 4.6 59.8 1.0
CA R:THR62 4.6 38.9 1.0
CB R:ASN60 4.6 48.1 1.0
C R:ASP56 4.7 56.6 1.0
HG2 R:GLU67 4.7 61.8 1.0
CG R:ASP64 4.7 49.3 1.0
HG3 R:GLU67 4.7 61.8 1.0
N R:ALA57 4.7 60.4 1.0
HB3 R:ASP64 4.8 64.9 1.0
HB3 R:ASN60 4.8 58.7 1.0
CA R:ASN60 4.8 45.5 1.0
HB2 R:GLU67 4.9 58.0 1.0
N R:GLY61 4.9 40.3 1.0
C R:ILE63 4.9 38.0 1.0
CA R:ASP58 4.9 61.5 1.0
C R:ASP58 5.0 61.0 1.0
HB3 R:ASP56 5.0 61.5 1.0

Reference:

M.Zhang, X.Y.Meng, M.Cui, J.M.Pascal, D.E.Logothetis, J.F.Zhang. Selective Phosphorylation Modulates the PIP2 Sensitivity of the Cam-Sk Channel Complex. Nat.Chem.Biol. V. 10 753 2014.
ISSN: ISSN 1552-4450
PubMed: 25108821
DOI: 10.1038/NCHEMBIO.1592
Page generated: Sun Jul 14 12:30:27 2024

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