Calcium in PDB 2ehb: The Structure of the C-Terminal Domain of the Protein Kinase ATSOS2 Bound to the Calcium Sensor ATSOS3

All present enzymatic activity of The Structure of the C-Terminal Domain of the Protein Kinase ATSOS2 Bound to the Calcium Sensor ATSOS3:
2.7.11.1;

The structure of The Structure of the C-Terminal Domain of the Protein Kinase ATSOS2 Bound to the Calcium Sensor ATSOS3, PDB code: 2ehb was solved by M.J.Sanchez-Barrena, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.89 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.137, 57.387, 141.896, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 25.9

The binding sites of Calcium atom in the The Structure of the C-Terminal Domain of the Protein Kinase ATSOS2 Bound to the Calcium Sensor ATSOS3 (pdb code 2ehb). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The Structure of the C-Terminal Domain of the Protein Kinase ATSOS2 Bound to the Calcium Sensor ATSOS3, PDB code: 2ehb:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the The Structure of the C-Terminal Domain of the Protein Kinase ATSOS2 Bound to the Calcium Sensor ATSOS3


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Structure of the C-Terminal Domain of the Protein Kinase ATSOS2 Bound to the Calcium Sensor ATSOS3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1001 b:19.8 occ:1.00 O A:LEU54 2.2 20.2 1.0 O A:SER46 2.3 23.7 1.0 OE2 A:GLU59 2.4 20.7 1.0 O A:ILE50 2.4 23.7 1.0 O A:HOH1005 2.4 26.4 1.0 OD1 A:ASP52 2.5 24.1 1.0 OE1 A:GLU59 2.5 18.3 1.0 CD A:GLU59 2.8 19.1 1.0 C A:SER46 3.3 24.1 1.0 C A:LEU54 3.4 19.7 1.0 CG A:ASP52 3.5 22.0 1.0 C A:ILE50 3.6 24.2 1.0 OD2 A:ASP52 3.8 19.6 1.0 CA A:SER46 4.0 24.6 1.0 N A:ASP52 4.1 23.5 1.0 N A:LEU54 4.2 21.1 1.0 N A:ILE50 4.3 22.9 1.0 ND1 A:HIS56 4.3 17.6 1.0 CG A:GLU59 4.3 18.1 1.0 N A:SER47 4.3 23.7 1.0 CA A:ILE50 4.3 23.3 1.0 N A:ILE55 4.3 19.7 1.0 CA A:LEU54 4.3 20.3 1.0 CA A:ILE55 4.4 19.2 1.0 CB A:ILE50 4.5 23.2 1.0 CB A:SER46 4.5 24.6 1.0 CA A:SER47 4.6 23.7 1.0 N A:ASP51 4.6 24.9 1.0 CB A:ASP52 4.7 22.0 1.0 N A:HIS56 4.7 18.0 1.0 CA A:ASP51 4.8 25.2 1.0 CE1 A:HIS56 4.8 19.3 1.0 CB A:LEU54 4.8 20.3 1.0 CA A:ASP52 4.8 23.0 1.0 N A:GLY53 4.9 22.9 1.0 O A:HOH1031 5.0 34.1 1.0 C A:ASP51 5.0 24.6 1.0

Calcium binding site 2 out of 2 in the The Structure of the C-Terminal Domain of the Protein Kinase ATSOS2 Bound to the Calcium Sensor ATSOS3


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Structure of the C-Terminal Domain of the Protein Kinase ATSOS2 Bound to the Calcium Sensor ATSOS3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1004 b:29.4 occ:1.00 OD1 A:ASP164 2.2 25.2 1.0 O A:LYS170 2.3 25.0 1.0 OD2 A:ASP168 2.4 32.8 1.0 OE1 A:GLU175 2.5 17.5 1.0 OE2 A:GLU175 2.5 16.3 1.0 O A:HOH1007 2.6 24.1 1.0 OD1 A:ASP168 2.6 35.0 1.0 CG A:ASP168 2.8 32.9 1.0 CD A:GLU175 2.8 17.8 1.0 O A:HOH1127 3.1 89.1 1.0 CG A:ASP164 3.3 25.3 1.0 C A:LYS170 3.4 25.0 1.0 OD2 A:ASP164 4.1 22.3 1.0 N A:LYS170 4.2 26.6 1.0 CB A:ASP164 4.2 25.0 1.0 CB A:ASP168 4.2 31.6 1.0 CA A:ASP164 4.2 25.4 1.0 CA A:ILE171 4.2 22.1 1.0 N A:ILE171 4.3 23.5 1.0 N A:ASP168 4.3 31.8 1.0 CB A:LYS166 4.3 30.0 1.0 CD A:LYS166 4.3 31.6 1.0 CG A:GLU175 4.3 17.7 1.0 CA A:LYS170 4.4 26.1 1.0 OD2 A:ASP172 4.4 26.6 1.0 N A:ASP172 4.5 22.5 1.0 N A:LYS166 4.6 29.3 1.0 C A:ASP164 4.6 26.1 1.0 N A:GLY169 4.7 29.2 1.0 CA A:ASP168 4.7 31.2 1.0 N A:ASN167 4.7 31.2 1.0 CG A:LYS166 4.8 30.6 1.0 CB A:LYS170 4.8 26.2 1.0 CA A:LYS166 4.8 29.9 1.0 C A:ILE171 4.8 22.4 1.0 C A:LYS166 4.9 30.4 1.0 O A:ASP164 4.9 25.7 1.0 C A:ASP168 5.0 30.7 1.0

M.J.Sanchez-Barrena, H.Fujii, I.Angulo, M.Martinez-Ripoll, J.K.Zhu, A.Albert. The Structure of the C-Terminal Domain of the Protein Kinase ATSOS2 Bound to the Calcium Sensor ATSOS3 Mol.Cell V. 26 427 2007.
ISSN: ISSN 1097-2765
PubMed: 17499048
DOI: 10.1016/J.MOLCEL.2007.04.013