Calcium in PDB 1a29: Calmodulin Complexed with Trifluoperazine (1:2 Complex)

The structure of Calmodulin Complexed with Trifluoperazine (1:2 Complex), PDB code: 1a29 was solved by Zs.Bocskei, V.Harmat, B.G.Vertessy, J.Ovadi, G.Naray-Szabo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.19 / 2.74
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	40.750, 40.750, 177.570, 90.00, 90.00, 120.00
R / Rfree (%)	19.7 / 26.5

The structure of Calmodulin Complexed with Trifluoperazine (1:2 Complex) also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Calcium atom in the Calmodulin Complexed with Trifluoperazine (1:2 Complex) (pdb code 1a29). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Calmodulin Complexed with Trifluoperazine (1:2 Complex), PDB code: 1a29:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Calmodulin Complexed with Trifluoperazine (1:2 Complex)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Calmodulin Complexed with Trifluoperazine (1:2 Complex) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca149 b:28.9 occ:1.00 O A:THR26 2.3 36.0 1.0 OD1 A:ASP20 2.3 36.9 1.0 OD1 A:ASP22 2.3 31.4 1.0 OE2 A:GLU31 2.3 17.8 1.0 OD1 A:ASP24 2.3 35.5 1.0 OE1 A:GLU31 2.3 17.8 1.0 CD A:GLU31 2.6 17.8 1.0 CG A:ASP22 3.2 31.4 1.0 CG A:ASP24 3.3 35.5 1.0 OD2 A:ASP22 3.4 31.4 1.0 C A:THR26 3.5 33.5 1.0 CG A:ASP20 3.5 36.9 1.0 OD2 A:ASP24 3.9 35.5 1.0 CA A:ASP20 4.1 14.8 1.0 CG A:GLU31 4.1 17.8 1.0 N A:THR26 4.2 33.5 1.0 CB A:ASP20 4.3 36.9 1.0 OG1 A:THR26 4.3 36.0 1.0 N A:ASP24 4.4 34.8 1.0 CA A:THR26 4.4 33.5 1.0 CB A:ASP24 4.4 35.5 1.0 OD2 A:ASP20 4.4 36.9 1.0 N A:ILE27 4.4 22.0 1.0 CA A:ILE27 4.5 22.0 1.0 N A:ASP22 4.5 32.8 1.0 CB A:ASP22 4.6 31.4 1.0 C A:ASP20 4.6 14.8 1.0 CG2 A:THR28 4.6 9.6 1.0 N A:THR28 4.7 12.2 1.0 N A:LYS21 4.7 23.8 1.0 N A:GLY23 4.7 31.0 1.0 CA A:ASP24 4.8 34.8 1.0 CA A:ASP22 4.9 32.8 1.0 N A:GLY25 4.9 25.3 1.0 CB A:THR26 5.0 36.0 1.0

Calcium binding site 2 out of 4 in the Calmodulin Complexed with Trifluoperazine (1:2 Complex)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Calmodulin Complexed with Trifluoperazine (1:2 Complex) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca150 b:42.6 occ:1.00 OE1 A:GLU67 2.3 33.2 1.0 OD1 A:ASN60 2.3 34.1 1.0 OD1 A:ASP56 2.3 47.4 1.0 OD1 A:ASP58 2.3 43.5 1.0 OE2 A:GLU67 2.3 33.2 1.0 O A:THR62 2.3 28.8 1.0 CD A:GLU67 2.6 33.2 1.0 CG A:ASP58 3.2 43.5 1.0 CG A:ASN60 3.2 34.1 1.0 CG A:ASP56 3.5 47.4 1.0 C A:THR62 3.5 31.9 1.0 OD2 A:ASP58 3.5 43.5 1.0 ND2 A:ASN60 3.7 34.1 1.0 OG1 A:THR62 4.0 28.8 1.0 OD2 A:ASP56 4.1 47.4 1.0 CG A:GLU67 4.1 33.2 1.0 N A:ILE63 4.3 36.5 1.0 N A:ASN60 4.3 30.0 1.0 N A:THR62 4.3 31.9 1.0 CA A:ILE63 4.3 36.5 1.0 OD2 A:ASP64 4.4 27.7 1.0 CA A:THR62 4.4 31.9 1.0 CB A:ASN60 4.5 34.1 1.0 CB A:ASP58 4.5 43.5 1.0 CB A:ASP56 4.6 47.4 1.0 N A:ASP64 4.6 26.3 1.0 N A:ASP58 4.6 45.8 1.0 CG A:ASP64 4.6 27.7 1.0 CA A:ASP56 4.7 56.0 1.0 N A:GLY59 4.8 71.6 1.0 OD1 A:ASP64 4.8 27.7 1.0 CA A:ASN60 4.8 30.0 1.0 CB A:THR62 4.9 28.8 1.0 N A:ALA57 4.9 48.5 1.0 C A:ILE63 4.9 36.5 1.0 CA A:ASP58 5.0 45.8 1.0 CD1 A:ILE63 5.0 25.0 1.0

Calcium binding site 3 out of 4 in the Calmodulin Complexed with Trifluoperazine (1:2 Complex)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Calmodulin Complexed with Trifluoperazine (1:2 Complex) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca151 b:27.9 occ:1.00 OD1 A:ASP93 2.3 14.3 1.0 OD1 A:ASP95 2.3 34.0 1.0 OD1 A:ASN97 2.3 17.9 1.0 O A:TYR99 2.3 18.4 1.0 OE2 A:GLU104 2.3 27.3 1.0 OE1 A:GLU104 2.3 27.3 1.0 CD A:GLU104 2.6 27.3 1.0 CG A:ASP95 3.2 34.0 1.0 OD2 A:ASP95 3.4 34.0 1.0 CG A:ASN97 3.5 17.9 1.0 C A:TYR99 3.5 15.2 1.0 CG A:ASP93 3.5 14.3 1.0 CG A:GLU104 4.1 27.3 1.0 CA A:ASP93 4.2 23.7 1.0 N A:TYR99 4.2 15.2 1.0 ND2 A:ASN97 4.3 17.9 1.0 CA A:TYR99 4.3 15.2 1.0 CB A:ASP93 4.4 14.3 1.0 N A:ASN97 4.4 17.1 1.0 OD2 A:ASP93 4.4 14.3 1.0 N A:ILE100 4.4 8.9 1.0 N A:ASP95 4.4 16.6 1.0 CB A:ASN97 4.4 17.9 1.0 C A:ASP93 4.5 23.7 1.0 N A:SER101 4.5 8.7 1.0 CB A:ASP95 4.5 34.0 1.0 CA A:ILE100 4.5 8.9 1.0 N A:LYS94 4.7 15.5 1.0 CB A:TYR99 4.8 18.4 1.0 N A:GLY96 4.8 19.1 1.0 CA A:ASN97 4.8 17.1 1.0 CA A:ASP95 4.9 16.6 1.0 N A:GLY98 4.9 15.3 1.0 O A:ASP93 5.0 14.3 1.0 OG A:SER101 5.0 14.9 1.0 C A:ILE100 5.0 8.9 1.0 CB A:GLU104 5.0 27.3 1.0

Calcium binding site 4 out of 4 in the Calmodulin Complexed with Trifluoperazine (1:2 Complex)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Calmodulin Complexed with Trifluoperazine (1:2 Complex) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca152 b:16.1 occ:1.00 O A:GLN135 2.3 13.8 1.0 OD1 A:ASP131 2.3 31.4 1.0 OD1 A:ASP133 2.3 17.5 1.0 OD1 A:ASP129 2.3 6.0 1.0 OE1 A:GLU140 2.3 22.4 1.0 OE2 A:GLU140 2.3 22.4 1.0 CD A:GLU140 2.7 22.4 1.0 CG A:ASP133 3.3 17.5 1.0 CG A:ASP131 3.3 31.4 1.0 C A:GLN135 3.4 15.8 1.0 CG A:ASP129 3.5 6.0 1.0 OD2 A:ASP131 3.6 31.4 1.0 OD2 A:ASP133 3.8 17.5 1.0 N A:GLN135 4.1 15.8 1.0 CG A:GLU140 4.2 22.4 1.0 N A:ASP133 4.2 14.7 1.0 N A:VAL136 4.3 10.5 1.0 CA A:ASP129 4.3 26.9 1.0 OD2 A:ASP129 4.3 6.0 1.0 CA A:VAL136 4.3 10.5 1.0 N A:ILE130 4.4 13.8 1.0 CA A:GLN135 4.4 15.8 1.0 CB A:ASP129 4.4 6.0 1.0 CB A:ASP133 4.4 17.5 1.0 N A:ASP131 4.4 11.0 1.0 N A:ASN137 4.5 14.2 1.0 N A:GLY132 4.5 14.4 1.0 CB A:ASP131 4.6 31.4 1.0 CA A:ASP133 4.7 14.7 1.0 N A:GLY134 4.8 2.8 1.0 C A:ASP129 4.8 26.9 1.0 CA A:ASP131 4.8 11.0 1.0 CB A:GLN135 4.9 13.8 1.0 C A:VAL136 4.9 10.5 1.0 C A:ASP131 5.0 11.0 1.0 C A:ASP133 5.0 14.7 1.0

B.G.Vertessy, V.Harmat, Z.Bocskei, G.Naray-Szabo, F.Orosz, J.Ovadi. Simultaneous Binding of Drugs with Different Chemical Structures to CA2+-Calmodulin: Crystallographic and Spectroscopic Studies. Biochemistry V. 37 15300 1998.
ISSN: ISSN 0006-2960
PubMed: 9799490
DOI: 10.1021/BI980795A