Bromine in PDB 9esy: CDK2-Cyclin A in Complex with Fraglite 16

All present enzymatic activity of CDK2-Cyclin A in Complex with Fraglite 16:
2.7.11.22;

The structure of CDK2-Cyclin A in Complex with Fraglite 16, PDB code: 9esy was solved by I.Hope, M.P.Martin, M.J.Waring, M.E.M.Noble, J.A.Endicott, N.J.Tatum, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.14 / 2.39
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.073, 133.635, 148.056, 90, 90, 90
R / Rfree (%)	25.6 / 26.2

The binding sites of Bromine atom in the CDK2-Cyclin A in Complex with Fraglite 16 (pdb code 9esy). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the CDK2-Cyclin A in Complex with Fraglite 16, PDB code: 9esy:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the CDK2-Cyclin A in Complex with Fraglite 16


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of CDK2-Cyclin A in Complex with Fraglite 16 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br601 b:59.5 occ:1.00 BR1 A:HH8601 0.0 59.5 1.0 C1 A:HH8601 1.9 35.1 1.0 C8 A:HH8601 2.9 27.6 1.0 C2 A:HH8601 2.9 33.6 1.0 C7 A:HH8601 3.2 24.9 1.0 CZ A:PHE109 3.7 24.1 1.0 CG1 A:VAL289 3.7 27.2 1.0 CE2 A:PHE109 4.0 22.4 1.0 C3 A:HH8601 4.2 30.1 1.0 C4 A:HH8601 4.2 29.6 1.0 O A:PHE286 4.5 24.4 1.0 C6 A:HH8601 4.5 25.6 1.0 CE1 A:PHE109 4.5 20.1 1.0 N1 A:HH8601 4.7 30.9 1.0 CD2 A:PHE109 5.0 23.2 1.0

Bromine binding site 2 out of 4 in the CDK2-Cyclin A in Complex with Fraglite 16


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of CDK2-Cyclin A in Complex with Fraglite 16 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br602 b:79.7 occ:1.00 BR1 A:HH8602 0.0 79.7 1.0 C1 A:HH8602 1.9 59.0 1.0 C8 A:HH8602 2.7 55.4 1.0 C2 A:HH8602 2.9 51.2 1.0 C7 A:HH8602 2.9 47.7 1.0 O A:LEU83 3.4 24.0 1.0 N A:LEU83 3.4 23.2 1.0 CD1 A:LEU134 3.8 22.4 1.0 CB A:ALA31 3.9 20.3 1.0 C4 A:HH8602 4.1 72.3 1.0 CD1 A:PHE82 4.1 22.0 1.0 CA A:LEU83 4.2 26.2 1.0 C3 A:HH8602 4.2 67.9 1.0 C A:LEU83 4.2 24.6 1.0 C6 A:HH8602 4.3 65.6 1.0 O A:GLU81 4.3 26.1 1.0 CD1 A:ILE10 4.3 26.1 1.0 CA A:PHE82 4.3 23.0 1.0 CB A:LEU83 4.3 25.8 1.0 C A:PHE82 4.4 21.0 1.0 CD2 A:LEU134 4.5 26.4 1.0 CE1 A:PHE82 4.5 20.9 1.0 N1 A:HH8602 4.6 87.5 1.0 CG A:LEU134 4.7 28.9 1.0 CD1 A:LEU83 4.8 34.7 1.0 CG A:PHE82 4.9 25.6 1.0

Bromine binding site 3 out of 4 in the CDK2-Cyclin A in Complex with Fraglite 16


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of CDK2-Cyclin A in Complex with Fraglite 16 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br501 b:118.5 occ:1.00 BR1 B:HH8501 0.0 118.5 1.0 C1 B:HH8501 1.9 103.3 1.0 C8 B:HH8501 2.8 107.8 1.0 C2 B:HH8501 3.0 85.8 1.0 C7 B:HH8501 3.0 90.7 1.0 CB B:GLN378 3.9 25.2 1.0 CG B:GLN378 4.1 23.6 1.0 C4 B:HH8501 4.1 108.5 1.0 NE2 B:GLN378 4.2 28.7 1.0 C3 B:HH8501 4.2 80.5 1.0 C6 B:HH8501 4.3 92.4 1.0 CD B:GLN378 4.4 27.3 1.0 O B:HOH643 4.4 29.5 1.0 N1 B:HH8501 4.7 84.9 1.0

Bromine binding site 4 out of 4 in the CDK2-Cyclin A in Complex with Fraglite 16


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of CDK2-Cyclin A in Complex with Fraglite 16 within 5.0Å range: probe atom residue distance (Å) B Occ C:Br601 b:122.9 occ:1.00 BR1 C:HH8601 0.0 122.9 1.0 C1 C:HH8601 1.9 60.1 1.0 C8 C:HH8601 2.8 46.3 1.0 C2 C:HH8601 2.9 47.0 1.0 C7 C:HH8601 3.0 42.6 1.0 CG1 C:VAL18 4.1 31.6 1.0 C4 C:HH8601 4.1 36.4 1.0 C3 C:HH8601 4.2 43.6 1.0 C6 C:HH8601 4.4 37.5 1.0 CB C:VAL18 4.5 35.3 1.0 O C:ILE10 4.6 46.1 1.0 N1 C:HH8601 4.7 42.0 1.0 CG2 C:VAL18 4.7 35.0 1.0 CD2 C:LEU134 4.9 21.4 1.0 CD1 C:ILE10 4.9 29.1 1.0

I.Hope, M.P.Martin, M.J.Waring, M.E.M.Noble, J.A.Endicott, N.J.Tatum. Crystallographic Fragment Screening of CDK2-Cyclin A: Fraglites Map Sites of Protein-Protein Interaction To Be Published.