Calcium in PDB 4kho: Structure of the Fact Complex Subunit SPT16M

The structure of Structure of the Fact Complex Subunit SPT16M, PDB code: 4kho was solved by T.Stuwe, M.Hondele, A.G.Ladurner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.14 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.550, 75.030, 142.720, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 23.6

The binding sites of Calcium atom in the Structure of the Fact Complex Subunit SPT16M (pdb code 4kho). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of the Fact Complex Subunit SPT16M, PDB code: 4kho:

Calcium binding site 1 out of 1 in the Structure of the Fact Complex Subunit SPT16M


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 Fact Complex Subunit SPT16M within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1001 b:28.1 occ:1.00 O B:ASP904 2.4 28.1 1.0 OD1 B:ASP904 2.4 31.7 1.0 OD1 B:ASP907 2.4 25.9 1.0 O A:HOH1220 2.5 34.2 1.0 OE1 A:GLU785 2.5 32.2 1.0 OE2 A:GLU782 2.5 28.8 1.0 OE1 A:GLU782 2.6 32.9 1.0 CD A:GLU782 2.9 29.1 1.0 C B:ASP904 3.4 29.5 1.0 CD A:GLU785 3.5 37.2 1.0 CG B:ASP904 3.5 36.5 1.0 CG B:ASP907 3.6 27.3 1.0 CA B:ASP904 3.8 27.1 1.0 CA B:ASP907 4.0 25.5 1.0 CB A:GLU785 4.2 30.2 1.0 OE2 A:GLU785 4.3 42.8 1.0 CB B:ASP904 4.3 28.9 1.0 CB B:ASP907 4.3 25.2 1.0 NZ A:LYS789 4.3 34.8 1.0 N B:ASP907 4.4 22.6 1.0 CG A:GLU785 4.4 31.3 1.0 OD2 B:ASP904 4.4 37.2 1.0 CG A:GLU782 4.4 26.8 1.0 OD2 B:ASP907 4.5 30.0 1.0 N B:SER905 4.6 24.7 1.0 O A:HOH1298 4.6 49.6 1.0 O A:HOH1221 4.6 40.5 1.0 O A:HOH1106 4.6 23.3 1.0 CE A:LYS789 5.0 36.5 1.0

M.Hondele, T.Stuwe, M.Hassler, F.Halbach, A.Bowman, E.T.Zhang, B.Nijmeijer, C.Kotthoff, V.Rybin, S.Amlacher, E.Hurt, A.G.Ladurner. Structural Basis of Histone H2A-H2B Recognition By the Essential Chaperone Fact. Nature V. 499 111 2013.
ISSN: ISSN 0028-0836
PubMed: 23698368
DOI: 10.1038/NATURE12242