Chlorine in PDB 4j9z: Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant and NS309

The structure of Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant and NS309, PDB code: 4j9z 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)	27.79 / 1.66
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	77.200, 66.850, 64.830, 90.00, 93.81, 90.00
R / Rfree (%)	19.1 / 22.1

The structure of Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant and NS309 also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Chlorine atom in the Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant and NS309 (pdb code 4j9z). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant and NS309, PDB code: 4j9z:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant and NS309


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant and NS309 within 5.0Å range: probe atom residue distance (Å) B Occ R:Cl201 b:55.8 occ:0.52 CL1 R:1KP201 0.0 55.8 0.5 C4 R:1KP201 1.8 32.1 0.5 CD1 B:LEU480 2.1 44.5 0.5 C5 R:1KP201 2.7 36.0 0.5 C3 R:1KP201 2.7 34.7 0.5 CG B:LEU480 3.1 41.8 0.5 CL R:1KP201 3.1 56.2 0.5 CD2 B:LEU480 3.3 41.3 0.5 CE1 R:PHE68 3.8 40.1 0.5 CD1 R:LEU32 3.8 46.0 0.7 CD1 R:PHE68 3.8 39.0 0.5 CE1 R:PHE68 3.8 40.5 0.5 CD2 R:LEU32 3.9 45.3 0.3 CD1 R:PHE68 3.9 37.8 0.5 CD1 R:ILE27 3.9 34.2 1.0 CD1 R:PHE19 3.9 40.8 1.0 C2 R:1KP201 4.1 35.8 0.5 C6 R:1KP201 4.1 36.7 0.5 CE1 R:PHE19 4.2 44.4 1.0 CD1 B:LEU480 4.2 25.0 0.5 CG R:PHE19 4.2 37.9 1.0 CD1 R:ILE63 4.4 43.4 1.0 SD R:MET71 4.5 54.6 0.5 CB B:LEU480 4.5 29.5 0.5 CB B:LEU480 4.5 25.3 0.5 C1 R:1KP201 4.6 36.8 0.5 CZ R:PHE19 4.6 42.1 1.0 CD2 R:PHE19 4.7 39.9 1.0 CG R:LEU32 4.7 41.6 0.3 CG B:LEU480 4.7 24.9 0.5 CD2 B:LEU480 4.7 29.4 0.5 CB R:PHE19 4.8 38.7 1.0 CE2 R:PHE19 4.9 44.3 1.0 CG2 R:ILE27 4.9 32.7 1.0 CD1 R:LEU32 5.0 43.0 0.3

Chlorine binding site 2 out of 2 in the Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant and NS309


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Calcium-Calmodulin Complexed with the Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant and NS309 within 5.0Å range: probe atom residue distance (Å) B Occ R:Cl201 b:56.2 occ:0.52 CL R:1KP201 0.0 56.2 0.5 C5 R:1KP201 1.7 36.0 0.5 C4 R:1KP201 2.7 32.1 0.5 C6 R:1KP201 2.7 36.7 0.5 CG R:MET51 3.0 47.4 0.5 CD1 R:ILE63 3.0 43.4 1.0 CD1 R:LEU32 3.1 43.0 0.3 CL1 R:1KP201 3.1 55.8 0.5 N1 R:1KP201 3.2 38.2 0.5 CD2 R:LEU32 3.3 44.8 0.7 SD R:MET51 3.4 51.4 0.5 CD1 B:LEU480 3.5 44.5 0.5 CG R:MET51 3.7 44.2 0.5 CD1 R:LEU32 3.8 46.0 0.7 CD1 B:LEU480 3.8 25.0 0.5 CG R:LEU32 3.9 41.6 0.3 CD2 R:LEU32 3.9 45.3 0.3 O R:MET51 3.9 37.4 1.0 C1 R:1KP201 3.9 36.8 0.5 C3 R:1KP201 4.0 34.7 0.5 CB R:MET51 4.0 35.7 0.5 CB R:MET51 4.0 32.6 0.5 C R:MET51 4.0 36.1 1.0 CG R:LEU32 4.1 42.2 0.7 SD R:MET71 4.2 54.6 0.5 CE R:MET71 4.3 70.3 0.5 N R:ILE52 4.3 30.9 1.0 CG1 R:ILE63 4.5 41.9 1.0 C2 R:1KP201 4.5 35.8 0.5 CA R:ILE52 4.5 28.7 1.0 C7 R:1KP201 4.5 33.2 0.5 CA R:MET51 4.6 33.5 0.5 CA R:MET51 4.7 33.3 0.5 CD1 R:ILE52 4.7 44.3 1.0 CG B:LEU480 4.8 41.8 0.5 C R:1KP201 4.9 38.6 0.5 CG1 R:ILE52 5.0 39.3 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