Calcium in PDB 1zuz: Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase

The structure of Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase, PDB code: 1zuz was solved by P.Kursula, J.Vahokoski, M.Wilmanns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.91
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	66.520, 34.030, 73.850, 90.00, 109.58, 90.00
R / Rfree (%)	19.1 / 24.8

The binding sites of Calcium atom in the Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase (pdb code 1zuz). 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 in Complex with A Mutant Peptide From Human Drp-1 Kinase, PDB code: 1zuz:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca151 b:28.4 occ:1.00 OD2 A:ASP20 2.3 40.3 1.0 O A:HOH5011 2.3 29.4 1.0 O A:THR26 2.4 41.2 1.0 OD1 A:ASP24 2.4 44.5 1.0 OD2 A:ASP22 2.4 40.6 1.0 OE1 A:GLU31 2.4 39.2 1.0 OE2 A:GLU31 2.4 41.6 1.0 CD A:GLU31 2.8 41.1 1.0 CG A:ASP22 3.3 41.0 1.0 CG A:ASP24 3.4 45.0 1.0 CG A:ASP20 3.5 44.9 1.0 C A:THR26 3.6 41.4 1.0 OD1 A:ASP22 3.7 43.5 1.0 OD2 A:ASP24 4.0 44.5 1.0 OG1 A:THR26 4.2 52.0 1.0 N A:ASP24 4.2 44.2 1.0 N A:THR26 4.2 42.7 1.0 CA A:ASP20 4.2 41.1 1.0 CG A:GLU31 4.3 41.4 1.0 OD1 A:ASP20 4.3 42.3 1.0 CB A:ASP24 4.4 43.5 1.0 CB A:ASP20 4.4 42.8 1.0 N A:ASP22 4.4 42.3 1.0 CA A:THR26 4.4 43.8 1.0 C A:ASP20 4.5 41.4 1.0 O A:HOH5053 4.5 43.0 1.0 N A:ILE27 4.5 39.5 1.0 N A:GLY23 4.6 41.7 1.0 CB A:ASP22 4.6 42.4 1.0 CA A:ILE27 4.6 39.7 1.0 CA A:ASP24 4.7 43.9 1.0 N A:LYS21 4.7 42.0 1.0 O A:HOH5029 4.8 31.4 1.0 N A:GLY25 4.8 42.5 1.0 CA A:ASP22 4.8 42.6 1.0 CG2 A:THR28 4.9 43.8 1.0 N A:THR28 4.9 40.0 1.0 C A:ASP22 4.9 42.8 1.0 CB A:THR26 5.0 45.6 1.0 C A:ASP24 5.0 42.6 1.0

Calcium binding site 2 out of 4 in the Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca152 b:25.4 occ:1.00 O A:THR62 2.3 40.2 1.0 OD1 A:ASP56 2.3 41.2 1.0 O A:HOH5012 2.3 26.9 1.0 OE2 A:GLU67 2.3 38.6 1.0 OD1 A:ASP58 2.5 44.8 1.0 OD1 A:ASN60 2.5 42.8 1.0 OE1 A:GLU67 2.6 38.1 1.0 CD A:GLU67 2.8 37.4 1.0 CG A:ASP58 3.4 48.4 1.0 CG A:ASP56 3.4 39.5 1.0 C A:THR62 3.5 40.4 1.0 CG A:ASN60 3.5 43.3 1.0 OD2 A:ASP58 3.7 48.0 1.0 ND2 A:ASN60 4.1 44.3 1.0 N A:THR62 4.2 41.3 1.0 O A:HOH5028 4.2 44.1 1.0 CA A:ASP56 4.2 41.3 1.0 OD2 A:ASP56 4.2 38.7 1.0 N A:ASN60 4.3 43.3 1.0 CB A:ASP56 4.3 40.9 1.0 CG A:GLU67 4.3 37.5 1.0 N A:ILE63 4.4 39.2 1.0 N A:ASP64 4.4 39.7 1.0 CA A:THR62 4.5 40.9 1.0 CA A:ILE63 4.5 39.3 1.0 N A:ASP58 4.5 47.3 1.0 C A:ASP56 4.6 42.6 1.0 CB A:ASP58 4.6 47.5 1.0 CB A:ASN60 4.6 44.5 1.0 N A:GLY59 4.7 46.6 1.0 N A:GLY61 4.7 43.2 1.0 OG1 A:THR62 4.7 39.0 1.0 CG A:ASP64 4.8 39.7 1.0 OD2 A:ASP64 4.8 43.2 1.0 CA A:ASN60 4.8 43.6 1.0 N A:ALA57 4.8 44.8 1.0 C A:ILE63 4.8 40.6 1.0 CA A:ASP58 4.9 47.6 1.0 C A:ASN60 4.9 45.2 1.0 C A:ASP58 5.0 47.3 1.0

Calcium binding site 3 out of 4 in the Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca153 b:44.2 occ:1.00 OE2 A:GLU104 2.3 41.2 1.0 O A:HOH5013 2.3 43.1 1.0 OD2 A:ASP93 2.3 44.5 1.0 O A:TYR99 2.4 40.9 1.0 OD1 A:ASN97 2.5 36.9 1.0 OD1 A:ASP95 2.5 42.9 1.0 OE1 A:GLU104 2.6 36.4 1.0 CD A:GLU104 2.8 38.2 1.0 CG A:ASP95 3.4 42.2 1.0 CG A:ASN97 3.4 40.3 1.0 C A:TYR99 3.5 40.8 1.0 CG A:ASP93 3.5 44.3 1.0 OD2 A:ASP95 3.8 41.6 1.0 N A:ASN97 4.2 40.9 1.0 ND2 A:ASN97 4.2 40.9 1.0 N A:TYR99 4.2 40.9 1.0 CG A:GLU104 4.3 37.6 1.0 N A:ASP95 4.3 42.6 1.0 CA A:ASP93 4.3 43.1 1.0 OD1 A:ASP93 4.3 45.5 1.0 N A:ILE100 4.4 41.1 1.0 CA A:TYR99 4.4 40.4 1.0 N A:GLY96 4.4 42.0 1.0 CB A:ASN97 4.4 40.9 1.0 O A:HOH5088 4.4 56.4 1.0 CA A:ILE100 4.4 40.3 1.0 CB A:ASP93 4.5 42.5 1.0 C A:ASP93 4.5 43.1 1.0 CB A:ASP95 4.5 42.0 1.0 N A:SER101 4.5 39.1 1.0 N A:LYS94 4.7 43.2 1.0 CA A:ASN97 4.7 40.9 1.0 CA A:ASP95 4.7 41.9 1.0 CB A:TYR99 4.8 41.0 1.0 N A:GLY98 4.8 40.3 1.0 C A:ASP95 4.9 41.9 1.0 O A:ASP93 4.9 43.1 1.0 C A:ILE100 5.0 39.4 1.0

Calcium binding site 4 out of 4 in the Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Calmodulin in Complex with A Mutant Peptide From Human Drp-1 Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca154 b:45.5 occ:1.00 OD1 A:ASP129 2.1 34.3 1.0 O A:HOH5014 2.3 45.4 1.0 OD2 A:ASP131 2.3 41.5 1.0 OD2 A:ASP133 2.4 34.2 1.0 OE2 A:GLU140 2.5 37.0 1.0 O A:GLN135 2.5 37.5 1.0 OE1 A:GLU140 2.6 34.1 1.0 CD A:GLU140 2.9 37.9 1.0 CG A:ASP129 3.3 41.2 1.0 CG A:ASP131 3.3 43.1 1.0 CG A:ASP133 3.3 37.3 1.0 C A:GLN135 3.6 38.3 1.0 OD1 A:ASP131 3.6 50.4 1.0 OD1 A:ASP133 3.8 39.5 1.0 CA A:ASP129 4.1 40.2 1.0 CB A:ASP129 4.1 39.8 1.0 N A:ASP133 4.1 37.0 1.0 OD2 A:ASP129 4.1 40.7 1.0 N A:GLN135 4.2 38.4 1.0 N A:GLY132 4.2 36.6 1.0 N A:ASP131 4.3 38.7 1.0 CG A:GLU140 4.4 37.4 1.0 N A:VAL136 4.4 37.6 1.0 CA A:VAL136 4.4 37.7 1.0 CA A:GLN135 4.5 39.0 1.0 CB A:ASP133 4.5 36.1 1.0 C A:ASP129 4.5 40.2 1.0 CB A:ASP131 4.5 40.2 1.0 N A:ASN137 4.5 38.6 1.0 N A:ILE130 4.6 39.3 1.0 CA A:ASP131 4.7 39.0 1.0 C A:ASP131 4.7 38.0 1.0 CA A:ASP133 4.7 37.0 1.0 N A:GLY134 4.8 37.4 1.0 CB A:GLN135 4.9 39.7 1.0 C A:ASP133 5.0 37.0 1.0 C A:VAL136 5.0 38.1 1.0

P.Kursula, J.Vahokoski, M.Wilmanns. Recognition of Human Death-Associated Protein Kinases By Calmodulin To Be Published.