Bromine in PDB 9esp: CDK2-Cyclin A in Complex with Fraglite 26

All present enzymatic activity of CDK2-Cyclin A in Complex with Fraglite 26:
2.7.11.22;

The structure of CDK2-Cyclin A in Complex with Fraglite 26, PDB code: 9esp 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)	99.33 / 2.38
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.064, 133.712, 147.734, 90, 90, 90
R / Rfree (%)	20.9 / 21.2

The binding sites of Bromine atom in the CDK2-Cyclin A in Complex with Fraglite 26 (pdb code 9esp). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the CDK2-Cyclin A in Complex with Fraglite 26, PDB code: 9esp:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the CDK2-Cyclin A in Complex with Fraglite 26


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 26 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1501 b:111.4 occ:1.00 BR A:UUV1501 0.0 111.4 1.0 C A:UUV1501 1.9 120.9 1.0 C1 A:UUV1501 2.9 93.6 1.0 C5 A:UUV1501 3.0 98.6 1.0 O A:HOH1692 3.1 62.7 1.0 O A:HOH1684 3.6 61.6 1.0 CG A:PHE80 3.6 38.3 1.0 CD2 A:PHE80 3.8 38.7 1.0 CB A:PHE80 3.9 38.4 1.0 CD1 A:PHE80 4.0 36.2 1.0 N A:UUV1501 4.0 89.3 1.0 N1 A:UUV1501 4.1 78.6 1.0 CE2 A:PHE80 4.2 42.9 1.0 CD1 A:LEU134 4.3 39.1 1.0 CG2 A:VAL64 4.4 40.6 1.0 CE1 A:PHE80 4.5 36.4 1.0 CZ A:PHE80 4.6 36.6 1.0 CB A:ALA31 4.6 38.2 1.0 CB A:ALA144 4.9 39.5 1.0 O A:GLU81 5.0 52.0 1.0 CE A:LYS33 5.0 76.4 1.0

Bromine binding site 2 out of 3 in the CDK2-Cyclin A in Complex with Fraglite 26


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 26 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br501 b:131.6 occ:1.00 BR B:UUV501 0.0 131.6 1.0 C B:UUV501 1.9 138.9 1.0 C1 B:UUV501 2.9 130.7 1.0 C5 B:UUV501 2.9 144.9 1.0 CD1 B:LEU214 3.9 45.8 1.0 CG B:GLN254 3.9 52.7 1.0 CD B:GLN254 4.0 55.6 1.0 CB B:GLN254 4.0 53.6 1.0 N B:UUV501 4.0 120.8 1.0 N1 B:UUV501 4.1 130.6 1.0 CA B:LEU214 4.1 45.2 1.0 OE1 B:GLN254 4.1 57.4 1.0 CB B:LEU214 4.4 41.5 1.0 NE2 B:GLN254 4.4 57.8 1.0 CG2 B:ILE213 4.5 47.8 1.0 CE3 B:TRP217 4.6 41.8 1.0 N B:LEU214 4.6 44.5 1.0 CB B:TRP217 4.6 43.8 1.0 CA B:GLN254 4.7 54.7 1.0 CD2 B:TRP217 4.7 43.0 1.0 O B:ILE213 4.7 47.8 1.0 CG B:TRP217 4.7 44.0 1.0 C B:ILE213 4.8 46.0 1.0 CG B:LEU214 4.8 42.5 1.0

Bromine binding site 3 out of 3 in the CDK2-Cyclin A in Complex with Fraglite 26


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 26 within 5.0Å range: probe atom residue distance (Å) B Occ C:Br501 b:83.8 occ:1.00 BR C:UUV501 0.0 83.8 1.0 C C:UUV501 1.9 75.6 1.0 C1 C:UUV501 2.9 71.0 1.0 C5 C:UUV501 2.9 64.5 1.0 O C:HOH638 3.5 56.9 1.0 CG C:PHE80 3.6 43.0 1.0 CD2 C:PHE80 3.8 43.0 1.0 CB C:PHE80 3.8 39.5 1.0 O C:HOH646 4.0 62.6 1.0 N C:UUV501 4.0 75.6 1.0 CD1 C:PHE80 4.0 44.1 1.0 N1 C:UUV501 4.1 64.4 1.0 CB C:ALA31 4.2 37.7 1.0 CE2 C:PHE80 4.3 42.9 1.0 CD1 C:LEU134 4.3 44.6 1.0 O C:HOH657 4.5 72.2 1.0 CG2 C:VAL64 4.5 39.8 1.0 CE1 C:PHE80 4.5 42.6 1.0 CZ C:PHE80 4.6 42.3 1.0 O C:GLU81 4.9 50.9 1.0 CE C:LYS33 4.9 59.9 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.