Fluorine in PDB 4a4x: NEK2-Ede Bound to CCT248662

All present enzymatic activity of NEK2-Ede Bound to CCT248662:
2.7.11.1;

The structure of NEK2-Ede Bound to CCT248662, PDB code: 4a4x was solved by C.Mas-Droux, R.Bayliss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.379 / 2.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.223, 56.909, 74.408, 90.00, 127.12, 90.00
R / Rfree (%)	20.42 / 24.69

The binding sites of Fluorine atom in the NEK2-Ede Bound to CCT248662 (pdb code 4a4x). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the NEK2-Ede Bound to CCT248662, PDB code: 4a4x:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the NEK2-Ede Bound to CCT248662


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of NEK2-Ede Bound to CCT248662 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1280 b:27.6 occ:1.00 F36 A:JUP1280 0.0 27.6 1.0 C35 A:JUP1280 1.4 32.0 1.0 F37 A:JUP1280 2.2 27.3 1.0 F38 A:JUP1280 2.2 28.3 1.0 C34 A:JUP1280 2.4 21.6 1.0 C02 A:JUP1280 3.0 31.1 1.0 OH A:TYR19 3.0 59.6 1.0 C01 A:JUP1280 3.0 31.8 1.0 C29 A:JUP1280 3.1 22.4 1.0 CB A:CYS22 3.3 30.1 1.0 C33 A:JUP1280 3.5 25.6 1.0 CA A:GLY15 3.6 37.6 1.0 SG A:CYS22 3.6 43.2 1.0 CZ A:TYR19 3.9 58.3 1.0 N A:GLY15 4.1 35.3 1.0 C A:GLY15 4.2 39.0 1.0 O03 A:JUP1280 4.3 24.3 1.0 C30 A:JUP1280 4.4 22.1 1.0 CE2 A:TYR19 4.4 45.8 1.0 O A:GLY15 4.5 35.2 1.0 CA A:CYS22 4.6 25.6 1.0 C05 A:JUP1280 4.7 26.1 1.0 N A:CYS22 4.7 36.3 1.0 C32 A:JUP1280 4.8 23.9 1.0 CG2 A:ILE14 4.8 37.5 1.0 CE1 A:TYR19 4.8 61.6 1.0 C A:ILE14 4.8 26.2 1.0 N A:THR16 4.9 56.9 1.0

Fluorine binding site 2 out of 3 in the NEK2-Ede Bound to CCT248662


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of NEK2-Ede Bound to CCT248662 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1280 b:27.3 occ:1.00 F37 A:JUP1280 0.0 27.3 1.0 C35 A:JUP1280 1.4 32.0 1.0 F36 A:JUP1280 2.2 27.6 1.0 F38 A:JUP1280 2.2 28.3 1.0 C34 A:JUP1280 2.4 21.6 1.0 C29 A:JUP1280 3.1 22.4 1.0 C02 A:JUP1280 3.1 31.1 1.0 C05 A:JUP1280 3.2 26.1 1.0 C33 A:JUP1280 3.4 25.6 1.0 CB A:CYS22 3.5 30.1 1.0 C08 A:JUP1280 3.6 25.4 1.0 SG A:CYS22 3.7 43.2 1.0 CG2 A:ILE14 3.8 37.5 1.0 O03 A:JUP1280 4.0 24.3 1.0 C01 A:JUP1280 4.0 31.8 1.0 C04 A:JUP1280 4.1 24.0 1.0 C07 A:JUP1280 4.1 25.4 1.0 C06 A:JUP1280 4.1 24.7 1.0 S18 A:JUP1280 4.1 35.1 1.0 C09 A:JUP1280 4.3 23.7 1.0 C30 A:JUP1280 4.4 22.1 1.0 CB A:ILE14 4.5 40.1 1.0 C10 A:JUP1280 4.5 24.5 1.0 C32 A:JUP1280 4.6 23.9 1.0 N A:GLY15 4.8 35.3 1.0 CA A:GLY15 4.9 37.6 1.0 CA A:CYS22 5.0 25.6 1.0

Fluorine binding site 3 out of 3 in the NEK2-Ede Bound to CCT248662


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of NEK2-Ede Bound to CCT248662 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1280 b:28.3 occ:1.00 F38 A:JUP1280 0.0 28.3 1.0 C35 A:JUP1280 1.3 32.0 1.0 F36 A:JUP1280 2.2 27.6 1.0 F37 A:JUP1280 2.2 27.3 1.0 C34 A:JUP1280 2.3 21.6 1.0 C33 A:JUP1280 2.6 25.6 1.0 CG2 A:ILE14 3.3 37.5 1.0 C29 A:JUP1280 3.6 22.4 1.0 CA A:GLY15 3.7 37.6 1.0 O A:ILE14 3.8 44.0 1.0 N A:GLY15 3.9 35.3 1.0 S18 A:JUP1280 3.9 35.1 1.0 C A:ILE14 3.9 26.2 1.0 C32 A:JUP1280 4.0 23.9 1.0 C02 A:JUP1280 4.3 31.1 1.0 CB A:ILE14 4.3 40.1 1.0 CB A:CYS22 4.7 30.1 1.0 OH A:TYR19 4.7 59.6 1.0 C30 A:JUP1280 4.7 22.1 1.0 C01 A:JUP1280 4.8 31.8 1.0 CA A:ILE14 4.8 26.9 1.0 C A:GLY15 4.9 39.0 1.0 C17 A:JUP1280 4.9 24.8 1.0 C08 A:JUP1280 4.9 25.4 1.0 C31 A:JUP1280 4.9 21.6 1.0 C10 A:JUP1280 5.0 24.5 1.0

P.Innocenti, K.M.Cheung, S.Solanki, C.Mas-Droux, F.Rowan, S.Yeoh, K.Boxall, M.Westlake, L.Pickard, T.Hardy, J.E.Baxter, G.W.Aherne, R.Bayliss, A.M.Fry, S.Hoelder. Design of Potent and Selective Hybrid Inhibitors of the Mitotic Kinase NEK2: Structure-Activity Relationship, Structural Biology, and Cellular Activity. J.Med.Chem. V. 55 3228 2012.
ISSN: ISSN 0022-2623
PubMed: 22404346
DOI: 10.1021/JM201683B