Chlorine in PDB 2f2c: X-Ray Structure of Human CDK6-Vcyclinwith the Inhibitor Aminopurvalanol

All present enzymatic activity of X-Ray Structure of Human CDK6-Vcyclinwith the Inhibitor Aminopurvalanol:
2.7.1.37;

The structure of X-Ray Structure of Human CDK6-Vcyclinwith the Inhibitor Aminopurvalanol, PDB code: 2f2c was solved by U.Schulze-Gahmen, H.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.80
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	71.517, 71.517, 449.297, 90.00, 90.00, 120.00
R / Rfree (%)	23.8 / 30.1

The binding sites of Chlorine atom in the X-Ray Structure of Human CDK6-Vcyclinwith the Inhibitor Aminopurvalanol (pdb code 2f2c). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the X-Ray Structure of Human CDK6-Vcyclinwith the Inhibitor Aminopurvalanol, PDB code: 2f2c:

Chlorine binding site 1 out of 1 in the X-Ray Structure of Human CDK6-Vcyclinwith the Inhibitor Aminopurvalanol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of Human CDK6-Vcyclinwith the Inhibitor Aminopurvalanol within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl401 b:80.1 occ:1.00 CL1 B:AP9401 0.0 80.1 1.0 C5A B:AP9401 1.5 80.2 1.0 C4A B:AP9401 2.5 79.9 1.0 C6A B:AP9401 2.5 79.8 1.0 OG1 B:THR107 3.1 71.3 1.0 OD1 B:ASP104 3.3 74.2 1.0 OD2 B:ASP104 3.4 74.2 1.0 CG B:ASP104 3.5 73.6 1.0 CB B:THR107 3.7 71.5 1.0 C3A B:AP9401 3.8 80.0 1.0 C1A B:AP9401 3.8 79.9 1.0 N B:ASP104 4.1 72.3 1.0 C2A B:AP9401 4.3 80.4 1.0 CG2 B:THR107 4.3 71.4 1.0 CB B:ASP104 4.5 72.8 1.0 CA B:GLN103 4.8 71.4 1.0 N10 B:AP9401 4.9 79.9 1.0 CA B:ASP104 4.9 72.7 1.0 N6 B:AP9401 4.9 80.3 1.0 C B:GLN103 4.9 71.8 1.0

H.Lu, U.Schulze-Gahmen. Toward Understanding the Structural Basis of Cyclin-Dependent Kinase 6 Specific Inhibition. J.Med.Chem. V. 49 3826 2006.
ISSN: ISSN 0022-2623
PubMed: 16789739
DOI: 10.1021/JM0600388