Fluorine in PDB 6fvf: The Structure of CK2ALPHA with CCH503 Bound

All present enzymatic activity of The Structure of CK2ALPHA with CCH503 Bound:
2.7.11.1;

The structure of The Structure of CK2ALPHA with CCH503 Bound, PDB code: 6fvf was solved by P.Brear, R.Prudent, B.Laudet, O.Filhol, C.Cochet, C.Sautel, V.Moucadel, B.Bestgen, M.Engel, M.Ettaoussi, T.Lomberget, M.Le Borgne, I.Kufareva, R.Abagyan, M.Hyvonen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.53 / 1.47
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.987, 45.250, 62.751, 90.00, 111.15, 90.00
R / Rfree (%)	20 / 22.2

The binding sites of Fluorine atom in the The Structure of CK2ALPHA with CCH503 Bound (pdb code 6fvf). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the The Structure of CK2ALPHA with CCH503 Bound, PDB code: 6fvf:

Fluorine binding site 1 out of 1 in the The Structure of CK2ALPHA with CCH503 Bound


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Structure of CK2ALPHA with CCH503 Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:47.9 occ:1.00 F A:503401 0.0 47.9 1.0 C5 A:503401 1.4 49.7 1.0 C6 A:503401 2.3 50.2 1.0 C4 A:503401 2.3 50.8 1.0 CB A:ALA110 3.1 33.7 1.0 OD1 A:ASP103 3.1 59.4 1.0 CG1 A:ILE69 3.1 34.4 1.0 CD1 A:ILE69 3.2 40.3 1.0 CB A:ASP103 3.6 48.7 1.0 C3 A:503401 3.6 53.7 1.0 C7 A:503401 3.6 52.7 1.0 CA A:ASP103 3.7 46.6 1.0 CG A:ASP103 3.8 59.6 1.0 CG1 A:VAL67 4.0 31.1 1.0 C2 A:503401 4.1 54.5 1.0 CG2 A:ILE69 4.2 33.9 1.0 CB A:ILE69 4.2 33.9 1.0 N A:ASP103 4.3 46.0 1.0 CA A:ALA110 4.5 32.9 1.0 CD A:PRO104 4.8 54.3 1.0 CG2 A:VAL101 4.9 37.8 1.0 C8 A:503401 5.0 54.9 1.0 C A:LYS102 5.0 47.9 1.0

R.Prudent, B.Laudet, O.Filhol, C.Cochet, C.Sautel, V.Moucadel, B.Bestgen, M.Engel, M.Ettaoussi, T.Lomberget, M.Le Borgne, I.Kufareva, R.Abagyan, P.Brear, M.Hyvonen. Structure-Based Discovery of Small Molecules Targeting the Flexible CK2 Subunit Interface To Be Published.