Calcium in PDB 4zlk: Crystal Structure of Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin

The structure of Crystal Structure of Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin, PDB code: 4zlk was solved by M.Shen, N.Zhang, S.Zheng, W.-B.Zhang, H.-M.Zhang, Z.Lu, Q.P.Su, Y.Sun, K.Ye, X.-D.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.85 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.079, 99.455, 248.159, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 24.6

The binding sites of Calcium atom in the Crystal Structure of Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin (pdb code 4zlk). 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 Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin, PDB code: 4zlk:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Crystal Structure of Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin


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 Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca201 b:83.5 occ:1.00 OD1 B:ASP22 2.0 83.9 1.0 OD1 B:ASP24 2.3 87.9 1.0 OE2 B:GLU31 2.4 71.9 1.0 O B:THR26 2.5 77.0 1.0 OE1 B:GLU31 2.6 78.2 1.0 CG B:ASP22 2.7 83.0 1.0 CD B:GLU31 2.8 73.4 1.0 OD1 B:ASP20 2.8 82.2 1.0 OD2 B:ASP22 2.9 81.5 1.0 CG B:ASP24 3.2 85.1 1.0 C B:THR26 3.7 79.6 1.0 OD2 B:ASP24 3.9 85.7 1.0 CG B:ASP20 4.0 83.8 1.0 CB B:ASP22 4.1 85.6 1.0 CB B:ASP24 4.1 79.9 1.0 N B:ASP22 4.2 81.3 1.0 CG B:GLU31 4.2 71.5 1.0 N B:ASP24 4.3 85.2 1.0 OG1 B:THR26 4.4 87.6 1.0 CA B:ASP20 4.5 81.8 1.0 N B:THR26 4.5 82.6 1.0 CA B:ASP22 4.6 83.3 1.0 N B:LYS21 4.6 84.2 1.0 N B:ILE27 4.6 80.2 1.0 CA B:ILE27 4.6 73.7 1.0 N B:GLY23 4.6 81.0 1.0 N B:THR28 4.6 68.0 1.0 C B:ASP20 4.7 85.6 1.0 CA B:THR26 4.7 82.5 1.0 CA B:ASP24 4.7 82.5 1.0 CB B:ASP20 4.8 80.5 1.0 CG2 B:THR28 4.8 70.7 1.0 C B:ASP22 4.8 81.8 1.0 OD2 B:ASP20 4.9 83.6 1.0

Calcium binding site 2 out of 4 in the Crystal Structure of Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin


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 Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca202 b:79.0 occ:1.00 OD1 B:ASN60 1.8 75.1 1.0 OD1 B:ASP58 2.0 80.0 1.0 O B:THR62 2.2 72.9 1.0 OD2 B:ASP56 2.2 80.8 1.0 OE2 B:GLU67 2.7 86.2 1.0 OE1 B:GLU67 2.8 83.2 1.0 CG B:ASN60 2.9 79.7 1.0 CG B:ASP58 2.9 80.4 1.0 CD B:GLU67 3.1 83.4 1.0 OD2 B:ASP58 3.1 86.7 1.0 CG B:ASP56 3.4 73.1 1.0 C B:THR62 3.4 73.2 1.0 ND2 B:ASN60 3.7 83.5 1.0 OD2 B:ASP64 3.8 92.3 1.0 CB B:ASN60 3.9 75.3 1.0 OG1 B:THR62 4.0 77.2 1.0 OD1 B:ASP56 4.1 72.4 1.0 N B:THR62 4.2 72.5 1.0 N B:ASN60 4.2 67.6 1.0 CA B:ILE63 4.2 79.9 1.0 CB B:ASP58 4.3 77.9 1.0 N B:ILE63 4.3 75.3 1.0 CA B:THR62 4.4 71.8 1.0 N B:ASP58 4.4 77.6 1.0 CB B:ASP56 4.5 65.5 1.0 CA B:ASN60 4.5 67.9 1.0 N B:ASP64 4.5 86.5 1.0 CA B:ASP56 4.5 69.1 1.0 CG B:ASP64 4.6 91.0 1.0 CG B:GLU67 4.6 84.9 1.0 CA B:ASP58 4.7 78.8 1.0 C B:ASN60 4.7 73.5 1.0 C B:ASP58 4.8 75.3 1.0 C B:ILE63 4.8 84.1 1.0 CB B:THR62 4.8 72.5 1.0 C B:ASP56 4.8 76.4 1.0 N B:ALA57 4.9 81.9 1.0 N B:GLY59 4.9 66.8 1.0 N B:GLY61 4.9 72.4 1.0

Calcium binding site 3 out of 4 in the Crystal Structure of Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin


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 Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca203 b:87.0 occ:1.00 OD2 B:ASP95 1.9 89.0 1.0 OD1 B:ASN97 2.0 86.3 1.0 OD2 B:ASP93 2.5 82.3 1.0 O B:TYR99 2.6 85.1 1.0 OE2 B:GLU104 2.7 79.9 1.0 CG B:ASP95 2.7 88.7 1.0 OE1 B:GLU104 2.7 88.0 1.0 CG B:ASN97 2.8 87.2 1.0 OD1 B:ASP95 2.9 90.1 1.0 CD B:GLU104 2.9 80.3 1.0 ND2 B:ASN97 3.4 81.6 1.0 CG B:ASP93 3.6 81.3 1.0 C B:TYR99 3.8 79.3 1.0 CB B:ASN97 4.0 88.5 1.0 CB B:ASP95 4.1 89.3 1.0 N B:ASN97 4.2 94.9 1.0 OD1 B:ASP93 4.3 83.5 1.0 CG B:GLU104 4.3 80.5 1.0 N B:TYR99 4.4 86.8 1.0 N B:ASP95 4.4 85.6 1.0 C B:ASP95 4.4 91.2 1.0 O B:ASP95 4.5 91.8 1.0 CA B:TYR99 4.5 82.1 1.0 CA B:ASN97 4.5 92.3 1.0 CA B:ASP95 4.6 89.6 1.0 N B:SER101 4.7 78.9 1.0 CB B:TYR99 4.7 81.3 1.0 N B:ILE100 4.7 74.8 1.0 CB B:ASP93 4.7 78.3 1.0 CA B:ILE100 4.8 72.0 1.0 CA B:ASP93 4.8 82.2 1.0 C B:ASN97 4.8 90.6 1.0 N B:GLY96 4.9 86.5 1.0

Calcium binding site 4 out of 4 in the Crystal Structure of Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin


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 Mouse Myosin-5A in Complex with Calcium-Bound Calmodulin within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca204 b:66.6 occ:1.00 OD2 B:ASP131 2.0 66.9 1.0 OD2 B:ASP133 2.1 69.2 1.0 OE1 B:GLU140 2.2 71.6 1.0 OD1 B:ASP129 2.3 66.0 1.0 O B:GLN135 2.5 64.6 1.0 OE2 B:GLU140 2.6 63.6 1.0 CD B:GLU140 2.8 64.0 1.0 CG B:ASP133 2.9 71.9 1.0 CG B:ASP131 3.0 67.5 1.0 OD1 B:ASP133 3.3 69.2 1.0 OD1 B:ASP131 3.3 65.8 1.0 CG B:ASP129 3.5 62.5 1.0 C B:GLN135 3.8 67.1 1.0 CB B:ASP133 4.0 73.6 1.0 N B:ASP133 4.1 67.2 1.0 ND2 B:ASN137 4.2 67.5 1.0 OD2 B:ASP129 4.3 62.2 1.0 CG B:GLU140 4.3 60.1 1.0 CB B:ASP131 4.3 61.0 1.0 N B:ASP131 4.4 61.0 1.0 CA B:ASP129 4.4 59.1 1.0 N B:GLN135 4.5 66.3 1.0 CB B:ASP129 4.5 60.4 1.0 CA B:ASP133 4.5 71.8 1.0 CA B:VAL136 4.6 70.0 1.0 C B:ASP131 4.6 65.3 1.0 N B:VAL136 4.6 69.4 1.0 N B:ASN137 4.7 67.3 1.0 CA B:ASP131 4.7 62.0 1.0 CA B:GLN135 4.7 70.5 1.0 N B:GLY132 4.7 61.6 1.0 C B:ASP129 4.8 62.0 1.0 C B:ASP133 4.8 74.6 1.0 CG B:ASN137 4.9 65.8 1.0 N B:GLY134 4.9 70.6 1.0 N B:ILE130 4.9 60.6 1.0 O B:ASP131 5.0 71.3 1.0

M.Shen, S.Zheng, W.Zhang, Z.Lu, K.Ye, X.Li. Structural Basis For Calcium Regulation of Myosin 5 Motor Function To Be Published.