Fluorine in PDB 3rpr: CDK2 in Complex with Inhibitor Rc-2-49

All present enzymatic activity of CDK2 in Complex with Inhibitor Rc-2-49:
2.7.11.22;

The structure of CDK2 in Complex with Inhibitor Rc-2-49, PDB code: 3rpr was solved by S.Betzi, R.Alam, H.Han, A.Becker, E.Schonbrunn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.84 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.398, 71.776, 72.976, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 21.7

The binding sites of Fluorine atom in the CDK2 in Complex with Inhibitor Rc-2-49 (pdb code 3rpr). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the CDK2 in Complex with Inhibitor Rc-2-49, PDB code: 3rpr:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the CDK2 in Complex with Inhibitor Rc-2-49


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of CDK2 in Complex with Inhibitor Rc-2-49 within 5.0Å range: probe atom residue distance (Å) B Occ A:F529 b:26.4 occ:1.00 F1 A:25Z529 0.0 26.4 1.0 C7 A:25Z529 1.4 24.4 1.0 F2 A:25Z529 2.2 26.4 1.0 F3 A:25Z529 2.3 26.7 1.0 C2 A:25Z529 2.3 23.0 1.0 C3 A:25Z529 2.7 20.1 1.0 CG2 A:ILE10 3.1 25.9 1.0 N A:GLY11 3.4 27.0 1.0 CB A:ILE10 3.5 25.8 1.0 CB A:VAL18 3.5 17.4 1.0 C A:ILE10 3.6 27.2 1.0 CA A:GLY11 3.6 27.3 1.0 C1 A:25Z529 3.7 20.7 1.0 CG1 A:VAL18 3.8 16.6 1.0 C A:GLY11 3.9 27.3 1.0 CG2 A:VAL18 4.0 16.8 1.0 O A:ILE10 4.0 28.2 1.0 O A:GLY11 4.1 27.1 1.0 CA A:ILE10 4.2 27.0 1.0 C4 A:25Z529 4.2 18.2 1.0 O A:HOH446 4.2 25.5 1.0 S1 A:25Z529 4.5 17.7 1.0 O A:VAL18 4.6 18.1 1.0 N A:GLU12 4.6 27.7 1.0 CA A:VAL18 4.7 17.8 1.0 CG1 A:ILE10 4.8 25.1 1.0 C6 A:25Z529 4.9 20.4 1.0 CD1 A:ILE10 4.9 24.2 1.0 C A:VAL18 5.0 18.1 1.0

Fluorine binding site 2 out of 3 in the CDK2 in Complex with Inhibitor Rc-2-49


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of CDK2 in Complex with Inhibitor Rc-2-49 within 5.0Å range: probe atom residue distance (Å) B Occ A:F529 b:26.4 occ:1.00 F2 A:25Z529 0.0 26.4 1.0 C7 A:25Z529 1.4 24.4 1.0 F1 A:25Z529 2.2 26.4 1.0 F3 A:25Z529 2.2 26.7 1.0 C2 A:25Z529 2.3 23.0 1.0 C1 A:25Z529 3.0 20.7 1.0 C A:GLU12 3.2 27.0 1.0 N A:GLY13 3.2 26.1 1.0 CG2 A:VAL18 3.3 16.8 1.0 O A:GLU12 3.3 26.6 1.0 C A:GLY11 3.4 27.3 1.0 CA A:GLY13 3.4 24.3 1.0 C3 A:25Z529 3.4 20.1 1.0 O A:GLY11 3.5 27.1 1.0 N A:GLU12 3.5 27.7 1.0 CB A:VAL18 3.6 17.4 1.0 CA A:GLU12 3.9 27.9 1.0 CA A:GLY11 3.9 27.3 1.0 N A:GLY11 4.3 27.0 1.0 C6 A:25Z529 4.3 20.4 1.0 CG1 A:VAL18 4.5 16.6 1.0 N A:VAL18 4.6 19.1 1.0 NE2 A:GLN131 4.6 26.3 1.0 C4 A:25Z529 4.7 18.2 1.0 CA A:VAL18 4.7 17.8 1.0 O A:HOH347 4.8 22.9 1.0 O A:HOH362 4.9 17.6 1.0 C A:GLY13 4.9 24.3 1.0 CD A:GLN131 4.9 24.2 1.0

Fluorine binding site 3 out of 3 in the CDK2 in Complex with Inhibitor Rc-2-49


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of CDK2 in Complex with Inhibitor Rc-2-49 within 5.0Å range: probe atom residue distance (Å) B Occ A:F529 b:26.7 occ:1.00 F3 A:25Z529 0.0 26.7 1.0 C7 A:25Z529 1.4 24.4 1.0 F2 A:25Z529 2.2 26.4 1.0 F1 A:25Z529 2.3 26.4 1.0 C2 A:25Z529 2.3 23.0 1.0 C1 A:25Z529 2.9 20.7 1.0 O A:HOH446 3.4 25.5 1.0 C3 A:25Z529 3.5 20.1 1.0 CD A:GLN131 3.8 24.2 1.0 CG A:GLN131 3.9 22.3 1.0 CA A:GLY11 4.0 27.3 1.0 O A:GLU12 4.0 26.6 1.0 OE1 A:GLN131 4.1 27.3 1.0 NE2 A:GLN131 4.2 26.3 1.0 C A:GLY11 4.2 27.3 1.0 N A:GLU12 4.2 27.7 1.0 C6 A:25Z529 4.3 20.4 1.0 C A:GLU12 4.5 27.0 1.0 N A:GLY11 4.5 27.0 1.0 O A:ILE10 4.6 28.2 1.0 CG2 A:ILE10 4.7 25.9 1.0 C4 A:25Z529 4.7 18.2 1.0 C A:ILE10 4.8 27.2 1.0 O A:GLY11 4.8 27.1 1.0 N A:GLY13 5.0 26.1 1.0

E.Schonbrunn, S.Betzi, R.Alam, M.P.Martin, A.Becker, H.Han, R.Francis, R.Chakrasali, S.Jakkaraj, A.Kazi, S.M.Sebti, C.L.Cubitt, A.W.Gebhard, L.A.Hazlehurst, J.S.Tash, G.I.Georg. Development of Highly Potent and Selective Diaminothiazole Inhibitors of Cyclin-Dependent Kinases. J.Med.Chem. V. 56 3768 2013.
ISSN: ISSN 0022-2623
PubMed: 23600925
DOI: 10.1021/JM301234K