Calcium in PDB 2fot: Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin

The structure of Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin, PDB code: 2fot was solved by M.Simonovic, Z.Zhang, C.D.Cianci, T.A.Steitz, J.S.Morrow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.48 / 2.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.288, 57.737, 69.753, 90.00, 90.00, 90.00
R / Rfree (%)	24.5 / 26.9

The binding sites of Calcium atom in the Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin (pdb code 2fot). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin, PDB code: 2fot:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca201 b:38.2 occ:1.00 OD1 A:ASP20 2.3 42.5 1.0 O A:THR26 2.3 42.1 1.0 OD2 A:ASP22 2.4 56.0 1.0 OE2 A:GLU31 2.5 37.8 1.0 OE1 A:GLU31 2.5 38.2 1.0 O A:HOH508 2.6 70.8 1.0 OD2 A:ASP24 2.7 45.9 1.0 CD A:GLU31 2.8 37.6 1.0 CG A:ASP20 3.5 43.9 1.0 CG A:ASP22 3.5 54.1 1.0 C A:THR26 3.5 41.6 1.0 CG A:ASP24 3.7 46.2 1.0 CA A:ASP20 3.7 45.3 1.0 OD1 A:ASP22 4.0 55.0 1.0 CB A:ASP20 4.1 44.6 1.0 C A:ASP20 4.1 47.1 1.0 N A:ASP24 4.1 46.9 1.0 N A:THR26 4.2 40.7 1.0 N A:LYS21 4.2 49.9 1.0 N A:ASP22 4.3 52.0 1.0 CG A:GLU31 4.3 35.6 1.0 OD1 A:ASP24 4.4 50.3 1.0 N A:GLY23 4.4 51.4 1.0 CA A:THR26 4.5 42.3 1.0 N A:ILE27 4.5 39.6 1.0 OD2 A:ASP20 4.5 41.9 1.0 CA A:ILE27 4.5 39.0 1.0 CB A:ASP24 4.6 46.1 1.0 OG1 A:THR26 4.7 44.5 1.0 CB A:ASP22 4.7 52.4 1.0 O A:ASP20 4.7 47.1 1.0 C A:ASP22 4.8 51.7 1.0 CA A:ASP24 4.8 45.3 1.0 CA A:ASP22 4.8 52.4 1.0 N A:GLY25 4.9 44.2 1.0 O A:PHE19 4.9 41.8 1.0 N A:ASP20 5.0 43.3 1.0 CG2 A:THR28 5.0 40.1 1.0

Calcium binding site 2 out of 4 in the Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca202 b:40.7 occ:1.00 O A:HOH551 2.2 36.3 1.0 OD1 A:ASP56 2.5 63.6 1.0 OE1 A:GLU67 2.6 41.3 1.0 O A:THR62 2.8 46.6 1.0 OE2 A:GLU67 2.8 43.6 1.0 CD A:GLU67 3.0 41.2 1.0 CB A:ASP58 3.1 71.1 1.0 OD1 A:ASN60 3.2 69.8 1.0 CG A:ASP56 3.7 62.6 1.0 CG A:ASN60 3.8 69.0 1.0 N A:ASP58 3.9 70.2 1.0 C A:THR62 4.0 47.1 1.0 CB A:ASN60 4.0 68.1 1.0 CA A:ASP58 4.1 70.3 1.0 CG A:ASP58 4.1 71.8 1.0 CA A:ASP56 4.4 61.4 1.0 CB A:ASP56 4.4 62.0 1.0 N A:GLY59 4.5 69.9 1.0 N A:ASN60 4.5 68.2 1.0 CG A:GLU67 4.5 38.3 1.0 OD2 A:ASP56 4.6 63.1 1.0 N A:ALA57 4.6 65.4 1.0 OD2 A:ASP58 4.7 72.6 1.0 CA A:ILE63 4.7 44.4 1.0 ND2 A:ASN60 4.7 70.2 1.0 N A:THR62 4.7 53.0 1.0 C A:ASP56 4.8 63.5 1.0 OG1 A:THR62 4.8 49.1 1.0 N A:ILE63 4.8 46.1 1.0 OD1 A:ASP58 4.8 70.6 1.0 N A:ASP64 4.8 40.2 1.0 C A:ASP58 4.8 70.4 1.0 CA A:ASN60 4.9 67.1 1.0 CA A:THR62 4.9 48.9 1.0 N A:GLY61 5.0 63.2 1.0

Calcium binding site 3 out of 4 in the Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca203 b:35.1 occ:1.00 O A:TYR99 2.2 33.1 1.0 OD2 A:ASP95 2.4 50.9 1.0 O A:HOH515 2.4 21.2 1.0 OE1 A:GLU104 2.4 45.6 1.0 OE2 A:GLU104 2.5 47.7 1.0 OD1 A:ASP93 2.6 33.9 1.0 OD1 A:ASN97 2.6 35.3 1.0 CD A:GLU104 2.8 46.6 1.0 CG A:ASP95 3.2 48.8 1.0 CG A:ASN97 3.3 39.1 1.0 C A:TYR99 3.4 32.6 1.0 OD1 A:ASP95 3.6 49.3 1.0 ND2 A:ASN97 3.8 36.9 1.0 CG A:ASP93 3.8 34.1 1.0 CG A:GLU104 4.2 47.1 1.0 N A:ASN97 4.3 44.4 1.0 N A:TYR99 4.3 32.0 1.0 CA A:ASP93 4.3 36.7 1.0 N A:ASP95 4.3 46.8 1.0 CA A:TYR99 4.3 33.4 1.0 N A:ILE100 4.3 31.9 1.0 CA A:ILE100 4.4 30.3 1.0 N A:SER101 4.4 32.7 1.0 CB A:ASN97 4.5 41.0 1.0 CB A:ASP95 4.5 47.4 1.0 C A:ASP93 4.5 38.5 1.0 CB A:ASP93 4.6 35.3 1.0 OD2 A:ASP93 4.7 31.9 1.0 N A:GLY96 4.7 46.9 1.0 CA A:ASP95 4.8 47.2 1.0 C A:ASP95 4.8 47.1 1.0 N A:LYS94 4.8 41.6 1.0 CB A:TYR99 4.8 33.1 1.0 CA A:ASN97 4.8 41.6 1.0 OG A:SER101 4.9 36.9 1.0 C A:ILE100 4.9 30.5 1.0 O A:ASP93 5.0 38.0 1.0

Calcium binding site 4 out of 4 in the Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Crystal Structure of the Complex Between Calmodulin and Alphaii-Spectrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca204 b:21.4 occ:1.00 OD2 A:ASP133 2.3 30.8 1.0 OE1 A:GLU140 2.3 25.2 1.0 O A:GLN135 2.4 31.8 1.0 OD1 A:ASP129 2.5 31.4 1.0 OD2 A:ASP131 2.5 20.8 1.0 OE2 A:GLU140 2.6 23.5 1.0 CD A:GLU140 2.8 25.4 1.0 CG A:ASP133 3.2 31.9 1.0 CG A:ASP131 3.3 22.0 1.0 OD1 A:ASP131 3.4 21.8 1.0 C A:GLN135 3.5 30.9 1.0 OD1 A:ASP133 3.6 31.4 1.0 CG A:ASP129 3.7 32.0 1.0 N A:ASP133 4.1 27.5 1.0 N A:GLN135 4.2 32.4 1.0 CG A:GLU140 4.3 24.8 1.0 CA A:ASP129 4.3 31.7 1.0 CA A:VAL136 4.3 27.5 1.0 CB A:ASP133 4.3 29.0 1.0 N A:VAL136 4.4 28.1 1.0 N A:GLY132 4.4 28.0 1.0 CB A:ASP129 4.5 31.2 1.0 N A:ASN137 4.5 27.1 1.0 CA A:GLN135 4.5 30.7 1.0 N A:ASP131 4.6 26.5 1.0 OD2 A:ASP129 4.6 32.8 1.0 CB A:ASP131 4.6 23.9 1.0 ND2 A:ASN137 4.6 29.0 1.0 CA A:ASP133 4.7 28.6 1.0 N A:GLY134 4.7 31.5 1.0 C A:ASP129 4.7 30.7 1.0 N A:ILE130 4.8 29.1 1.0 C A:VAL136 4.8 27.0 1.0 CG A:ASN137 4.9 30.9 1.0 CA A:ASP131 4.9 25.9 1.0 C A:ASP133 5.0 30.6 1.0 C A:ASP131 5.0 27.5 1.0

M.Simonovic, Z.Zhang, C.D.Cianci, T.A.Steitz, J.S.Morrow. Structure of the Calmodulin Alphaii-Spectrin Complex Provides Insight Into the Regulation of Cell Plasticity. J.Biol.Chem. V. 281 34333 2006.
ISSN: ISSN 0021-9258
PubMed: 16945920
DOI: 10.1074/JBC.M604613200