Fluorine in PDB 9i68: Crystal Structure of Human CDC20 Bound to Synthetic D-Box Peptide D21

The structure of Crystal Structure of Human CDC20 Bound to Synthetic D-Box Peptide D21, PDB code: 9i68 was solved by R.Eapen, C.Okoye, C.Stubbs, M.Schimpl, T.Tischer, E.J.Fisher, M.Zacharopoulou, F.Ferrer, D.Barford, D.Spring, C.Lindon, C.Phillips, L.S.Itzhaki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.73 / 1.51
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	35.491, 87.55, 48.573, 90, 109.71, 90
R / Rfree (%)	17.5 / 19.4

The binding sites of Fluorine atom in the Crystal Structure of Human CDC20 Bound to Synthetic D-Box Peptide D21 (pdb code 9i68). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Human CDC20 Bound to Synthetic D-Box Peptide D21, PDB code: 9i68:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Human CDC20 Bound to Synthetic D-Box Peptide D21


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human CDC20 Bound to Synthetic D-Box Peptide D21 within 5.0Å range: probe atom residue distance (Å) B Occ B:F4 b:28.1 occ:1.00 FAC B:3EG4 0.0 28.1 1.0 CG B:3EG4 1.3 28.0 1.0 FAE B:3EG4 2.1 28.5 1.0 FAD B:3EG4 2.1 27.9 1.0 CB B:3EG4 2.3 27.5 1.0 N B:3EG4 2.8 27.3 1.0 CA B:3EG4 2.9 27.5 1.0 C B:PRO3 3.2 28.5 1.0 CB A:TYR207 3.5 17.6 1.0 O B:PRO3 3.8 27.4 1.0 CD1 A:LEU202 3.8 20.2 1.0 CB B:PRO3 3.9 31.1 1.0 CG A:TYR207 3.9 19.9 1.0 CA B:PRO3 4.0 30.2 1.0 O A:ASP177 4.1 26.9 1.0 CB A:VAL200 4.3 19.0 1.0 C B:3EG4 4.4 28.8 1.0 CD1 A:TYR207 4.4 21.4 1.0 CG2 A:VAL200 4.5 20.7 1.0 CD2 A:TYR207 4.5 21.7 1.0 CG1 A:VAL200 4.6 20.2 1.0 CG A:LEU202 4.8 19.9 1.0 CA A:TYR207 4.9 16.9 1.0 CG2 A:ILE216 5.0 26.2 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Human CDC20 Bound to Synthetic D-Box Peptide D21


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Human CDC20 Bound to Synthetic D-Box Peptide D21 within 5.0Å range: probe atom residue distance (Å) B Occ B:F4 b:27.9 occ:1.00 FAD B:3EG4 0.0 27.9 1.0 CG B:3EG4 1.3 28.0 1.0 FAC B:3EG4 2.1 28.1 1.0 FAE B:3EG4 2.1 28.5 1.0 CB B:3EG4 2.3 27.5 1.0 CB A:TYR207 3.5 17.6 1.0 CB A:TRP209 3.6 19.6 1.0 CA B:3EG4 3.7 27.5 1.0 CG2 A:VAL200 3.8 20.7 1.0 N A:TRP209 4.1 18.0 1.0 C A:TYR207 4.1 16.3 1.0 O A:TYR207 4.1 15.9 1.0 CB A:VAL200 4.1 19.0 1.0 C A:LEU208 4.2 18.2 1.0 N B:3EG4 4.3 27.3 1.0 CA A:TRP209 4.4 19.1 1.0 N A:LEU208 4.4 15.7 1.0 CA A:TYR207 4.5 16.9 1.0 CG A:TYR207 4.5 19.9 1.0 O A:LEU208 4.5 19.4 1.0 CG A:TRP209 4.5 21.3 1.0 CG2 A:ILE216 4.6 26.2 1.0 C B:PRO3 4.7 28.5 1.0 CA A:LEU208 4.7 16.5 1.0 O B:PRO3 4.8 27.4 1.0 C B:3EG4 4.8 28.8 1.0 CD1 A:TRP209 4.9 23.1 1.0 CG1 A:VAL200 5.0 20.2 1.0 O B:3EG4 5.0 28.0 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Human CDC20 Bound to Synthetic D-Box Peptide D21


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Human CDC20 Bound to Synthetic D-Box Peptide D21 within 5.0Å range: probe atom residue distance (Å) B Occ B:F4 b:28.5 occ:1.00 FAE B:3EG4 0.0 28.5 1.0 CG B:3EG4 1.3 28.0 1.0 FAC B:3EG4 2.1 28.1 1.0 FAD B:3EG4 2.1 27.9 1.0 CB B:3EG4 2.4 27.5 1.0 CA B:3EG4 2.9 27.5 1.0 N B:3EG4 3.5 27.3 1.0 CG2 A:VAL200 3.6 20.7 1.0 O A:ASP177 4.0 26.9 1.0 CB A:VAL200 4.1 19.0 1.0 C B:3EG4 4.1 28.8 1.0 CD1 A:LEU176 4.2 27.0 1.0 CB A:LEU176 4.3 24.4 1.0 CG1 A:VAL200 4.3 20.2 1.0 O B:3EG4 4.4 28.0 1.0 CD2 A:LEU467 4.4 30.8 1.0 C B:PRO3 4.5 28.5 1.0 CB A:TRP209 4.6 19.6 1.0 CG A:LEU176 4.9 26.5 1.0

R.Eapen, C.Okoye, C.Stubbs, M.Schimpl, T.Tischer, E.J.Fisher, M.Zacharopoulou, F.Ferrer, D.Barford, D.Spring, C.Lindon, C.Phillips, L.S.Itzhaki. Development of D-Box Peptides to Inhibit the Anaphase Promoting Complex/Cyclosome To Be Published.