Potassium in PDB 3v8o: Human Filamin C Ig - Like Domains 4 and 5

The structure of Human Filamin C Ig - Like Domains 4 and 5, PDB code: 3v8o was solved by R.Sethi, J.Ylanne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.63 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.620, 91.350, 103.720, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 25.5

The binding sites of Potassium atom in the Human Filamin C Ig - Like Domains 4 and 5 (pdb code 3v8o). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Human Filamin C Ig - Like Domains 4 and 5, PDB code: 3v8o:

Potassium binding site 1 out of 1 in the Human Filamin C Ig - Like Domains 4 and 5


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Filamin C Ig - Like Domains 4 and 5 within 5.0Å range: probe atom residue distance (Å) B Occ A:K801 b:30.8 occ:1.00 O A:PRO653 2.6 30.0 1.0 O A:ASP651 2.7 30.0 1.0 O B:ASP651 2.7 28.0 1.0 C A:PRO653 3.6 30.0 1.0 C B:ASP651 3.7 29.2 1.0 C A:ASP651 3.7 30.0 1.0 O B:PRO653 3.7 20.2 1.0 O B:HOH821 3.8 30.9 1.0 CA A:PHE654 3.9 19.9 1.0 CA B:PHE654 3.9 19.7 1.0 CB A:ASP651 4.0 20.0 1.0 N A:PHE654 4.1 20.6 1.0 CD1 A:PHE654 4.2 13.9 1.0 C B:PRO653 4.2 20.9 1.0 CD1 B:PHE654 4.2 14.1 1.0 CA A:ASP651 4.2 30.0 1.0 CA B:ASP651 4.3 31.9 1.0 N B:PHE654 4.3 20.5 1.0 CB B:ASP651 4.5 32.6 1.0 CG B:PHE654 4.5 17.2 1.0 CB B:PHE654 4.5 18.8 1.0 CG A:PHE654 4.6 16.8 1.0 CE1 A:PHE654 4.6 14.2 1.0 N B:SER652 4.7 26.5 1.0 CB A:PHE654 4.8 18.8 1.0 N A:SER652 4.8 30.0 1.0 N A:ILE655 4.8 20.4 1.0 N B:ILE655 4.8 20.7 1.0 C A:PHE654 4.8 20.5 1.0 CE1 B:PHE654 4.9 13.8 1.0 CA A:PRO653 4.9 30.0 1.0 C B:PHE654 4.9 20.8 1.0 CA B:SER652 5.0 24.6 1.0

R.Sethi, J.Seppala, H.Tossavainen, M.Ylilauri, S.Ruskamo, O.T.Pentikainen, U.Pentikainen, P.Permi, J.Ylanne. A Novel Structural Unit in the N-Terminal Region of Filamins. J.Biol.Chem. V. 289 8588 2014.
ISSN: ISSN 0021-9258
PubMed: 24469451
DOI: 10.1074/JBC.M113.537456