Calcium in PDB 2xfv: Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6

The structure of Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6, PDB code: 2xfv was solved by S.J.Smerdon, D.C.Goldstone, I.A.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.784 / 1.90
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	69.934, 69.934, 297.944, 90.00, 90.00, 120.00
R / Rfree (%)	17.05 / 19.62

The structure of Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6 also contains other interesting chemical elements:

Arsenic

(As)

1 atom

The binding sites of Calcium atom in the Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6 (pdb code 2xfv). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6, PDB code: 2xfv:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1110 b:35.9 occ:1.00 O B:ASP102 2.5 31.0 1.0 OE1 A:GLU107 2.5 33.9 1.0 O B:HOH2145 2.6 32.5 1.0 O B:HOH2150 2.6 31.7 1.0 O A:HOH2076 2.7 50.4 1.0 O A:HOH2167 2.7 35.9 1.0 O B:HOH2152 2.8 51.0 1.0 CD A:GLU107 3.7 36.5 1.0 C B:ASP102 3.7 33.2 1.0 CB A:GLU107 4.1 31.3 1.0 O A:HOH2145 4.3 32.1 1.0 OE2 B:GLU105 4.3 38.5 1.0 O A:HOH2065 4.4 59.5 1.0 O A:HOH2163 4.5 43.5 1.0 NH2 B:ARG8 4.5 32.1 1.0 CG A:GLU107 4.5 32.0 1.0 OE2 A:GLU107 4.6 33.2 1.0 N B:ALA103 4.6 28.7 1.0 CA B:ALA103 4.6 31.1 1.0 CB B:ASP102 4.6 31.4 1.0 CA B:ASP102 4.6 35.8 1.0 O B:HOH2148 5.0 25.3 1.0 CG B:ASP102 5.0 37.9 1.0

Calcium binding site 2 out of 3 in the Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1111 b:29.3 occ:1.00 O A:HOH2133 3.0 16.4 1.0 O A:HOH2044 3.1 28.3 1.0 O A:HOH2137 3.3 13.9 1.0 NH1 A:ARG61 3.3 24.5 1.0 CD A:ARG61 3.7 22.6 1.0 CB A:LYS32 3.8 16.8 1.0 CD2 A:LEU31 3.9 13.8 1.0 CA A:LYS32 3.9 15.3 1.0 CD1 A:LEU35 3.9 18.8 1.0 N A:LYS32 4.0 13.2 1.0 CG A:LEU31 4.2 17.0 1.0 O A:HOH2045 4.2 46.5 1.0 CZ A:ARG61 4.3 23.5 1.0 CD1 A:LEU80 4.3 17.2 1.0 CB A:LEU31 4.3 15.8 1.0 CB A:LEU80 4.3 15.6 1.0 O A:HOH2136 4.4 45.1 1.0 NE A:ARG61 4.4 20.6 1.0 CG A:LEU80 4.5 15.1 1.0 C A:LEU31 4.6 15.4 1.0 O A:HOH2096 4.9 30.0 1.0 CG A:ARG61 4.9 19.8 1.0 CG A:LEU35 5.0 15.2 1.0

Calcium binding site 3 out of 3 in the Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1110 b:28.8 occ:1.00 O B:HOH2094 3.0 33.1 1.0 O B:HOH2122 3.1 19.6 1.0 O B:HOH2120 3.1 21.6 1.0 NH1 B:ARG61 3.3 26.1 1.0 CD1 B:LEU35 3.8 22.8 1.0 CD B:ARG61 3.8 24.0 1.0 CD2 B:LEU31 3.8 16.7 1.0 CA B:LYS32 3.9 25.2 1.0 N B:LYS32 3.9 18.7 1.0 CB B:LYS32 4.0 32.3 1.0 CG B:LEU31 4.1 14.9 1.0 CB B:LEU31 4.2 17.3 1.0 CZ B:ARG61 4.3 28.5 1.0 CB B:LEU80 4.3 16.2 1.0 CD1 B:LEU80 4.4 19.9 1.0 NE B:ARG61 4.5 24.1 1.0 CG B:LYS32 4.5 44.7 1.0 C B:LEU31 4.5 18.8 1.0 CG B:LEU80 4.6 23.4 1.0 O B:HOH2121 4.7 28.0 1.0 CG B:LEU35 4.9 24.3 1.0 N B:LEU80 4.9 18.1 1.0 CA B:LEU31 4.9 18.8 1.0

I.A.Taylor, D.C.Goldstone, P.Pala, L.Haire, S.J.Smerdon. Structure of the Amino-Terminal Domain From the Cell-Cycle Regulator SWI6S Proteins V. 78 2861 2010.
ISSN: ISSN 0887-3585
PubMed: 20635421
DOI: 10.1002/PROT.22795