Calcium in PDB 4j9y: Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant

The structure of Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant, PDB code: 4j9y was solved by M.Zhang, J.M.Pascal, J.-F.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.88 / 1.51
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	77.630, 66.820, 64.830, 90.00, 94.48, 90.00
R / Rfree (%)	18.3 / 21.6

The binding sites of Calcium atom in the Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant (pdb code 4j9y). 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 Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant, PDB code: 4j9y:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant within 5.0Å range: probe atom residue distance (Å) B Occ R:Ca1001 b:31.3 occ:1.00 O R:THR26 2.3 30.4 1.0 OE1 R:GLU31 2.3 24.9 1.0 OD1 R:ASP24 2.3 33.2 1.0 OD1 R:ASP20 2.4 31.4 1.0 OD1 R:ASP22 2.5 41.4 1.0 O R:HOH1101 2.5 36.7 1.0 OE2 R:GLU31 2.6 31.8 1.0 CD R:GLU31 2.8 36.9 1.0 CG R:ASP24 3.3 40.0 1.0 CG R:ASP22 3.3 36.0 1.0 C R:THR26 3.5 26.3 1.0 CG R:ASP20 3.5 35.8 1.0 OD2 R:ASP22 3.6 51.7 1.0 OD2 R:ASP24 3.8 42.5 1.0 CG2 R:THR26 4.0 33.1 1.0 N R:THR26 4.1 32.8 1.0 N R:ASP24 4.2 40.1 1.0 CA R:ASP20 4.2 27.4 1.0 CG R:GLU31 4.3 29.6 1.0 CB R:ASP20 4.3 30.6 1.0 CB R:ASP24 4.3 42.0 1.0 N R:ASP22 4.3 44.0 1.0 CA R:THR26 4.3 27.3 1.0 OD2 R:ASP20 4.4 32.7 1.0 C R:ASP20 4.4 36.8 1.0 N R:ILE27 4.4 26.4 1.0 CA R:ILE27 4.5 24.7 1.0 N R:GLY23 4.5 42.0 1.0 N R:LYS21 4.6 42.2 1.0 CB R:ASP22 4.6 37.0 1.0 CA R:ASP24 4.7 39.5 1.0 CA R:ASP22 4.8 44.9 1.0 N R:GLY25 4.8 34.9 1.0 O R:HOH1157 4.8 48.7 1.0 CB R:THR26 4.8 37.6 1.0 C R:ASP22 4.9 43.4 1.0 N R:THR28 4.9 24.8 1.0 O R:ASP20 4.9 37.9 1.0 C R:ASP24 4.9 38.7 1.0 CG2 R:THR28 5.0 30.0 1.0

Calcium binding site 2 out of 2 in the Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant within 5.0Å range: probe atom residue distance (Å) B Occ R:Ca1002 b:31.0 occ:1.00 O R:HOH1102 1.8 23.9 1.0 OD1 R:ASP56 2.2 33.4 1.0 OD2 R:ASP58 2.3 32.9 1.0 O R:THR62 2.5 26.4 1.0 OE1 R:GLU67 2.5 33.6 1.0 OE2 R:GLU67 2.5 37.5 1.0 OD1 R:ASN60 2.6 35.7 1.0 CD R:GLU67 2.9 35.5 1.0 CG R:ASP56 3.3 32.9 1.0 CG R:ASP58 3.4 36.2 1.0 CG R:ASN60 3.5 45.0 1.0 O R:HOH1259 3.6 40.1 1.0 C R:THR62 3.7 25.0 1.0 O R:HOH1186 3.8 30.6 1.0 OD1 R:ASP58 3.9 43.7 1.0 CA R:ASP56 3.9 46.0 1.0 CB R:ASP56 4.1 34.7 1.0 ND2 R:ASN60 4.1 51.8 1.0 OD2 R:ASP56 4.2 40.1 1.0 N R:ASP58 4.2 47.1 1.0 N R:ASN60 4.2 41.4 1.0 C R:ASP56 4.2 47.2 1.0 N R:ALA57 4.3 49.1 1.0 N R:THR62 4.4 29.7 1.0 CG R:GLU67 4.4 33.2 1.0 N R:GLY59 4.4 41.7 1.0 CB R:ASN60 4.6 47.5 1.0 CB R:ASP58 4.6 47.3 1.0 N R:ILE63 4.6 26.9 1.0 CA R:ILE63 4.6 25.1 1.0 CA R:THR62 4.7 29.6 1.0 CA R:ASP58 4.7 50.6 1.0 N R:GLY61 4.7 33.5 1.0 C R:ASP58 4.7 43.9 1.0 N R:ASP64 4.8 27.8 1.0 CA R:ASN60 4.8 37.5 1.0 O R:ASP56 4.8 47.9 1.0 OG1 R:THR62 4.9 29.7 1.0 C R:ASN60 5.0 37.7 1.0

M.Zhang, J.M.Pascal, J.F.Zhang. Unstructured to Structured Transition of An Intrinsically Disordered Protein Peptide in Coupling CA2+-Sensing and Sk Channel Activation. Proc.Natl.Acad.Sci.Usa V. 110 4828 2013.
ISSN: ISSN 0027-8424
PubMed: 23487779
DOI: 10.1073/PNAS.1220253110