Calcium in PDB 2euf: X-Ray Structure of Human CDK6-Vcyclin in Complex with the Inhibitor PD0332991

All present enzymatic activity of X-Ray Structure of Human CDK6-Vcyclin in Complex with the Inhibitor PD0332991:
2.7.1.37;

The structure of X-Ray Structure of Human CDK6-Vcyclin in Complex with the Inhibitor PD0332991, PDB code: 2euf 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 / 3.00
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	71.146, 71.146, 446.876, 90.00, 90.00, 120.00
R / Rfree (%)	22.9 / 30.6

The binding sites of Calcium atom in the X-Ray Structure of Human CDK6-Vcyclin in Complex with the Inhibitor PD0332991 (pdb code 2euf). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the X-Ray Structure of Human CDK6-Vcyclin in Complex with the Inhibitor PD0332991, PDB code: 2euf:

Calcium binding site 1 out of 1 in the X-Ray Structure of Human CDK6-Vcyclin in Complex with the Inhibitor PD0332991


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of X-Ray Structure of Human CDK6-Vcyclin in Complex with the Inhibitor PD0332991 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca255 b:70.8 occ:1.00 OG1 A:THR110 3.2 55.4 1.0 N A:LYS112 3.6 56.4 1.0 CG1 A:VAL111 3.8 56.0 1.0 CB A:LYS112 3.8 56.5 1.0 O A:LYS112 3.9 56.4 1.0 CA A:LYS112 4.1 56.5 1.0 CB B:ALA175 4.2 49.8 1.0 N A:VAL111 4.3 56.1 1.0 C A:LYS112 4.4 56.6 1.0 CB A:THR110 4.4 54.9 1.0 CG2 A:THR110 4.4 54.7 1.0 OD1 A:ASP69 4.5 57.8 1.0 C A:VAL111 4.7 56.4 1.0 O A:GLU67 4.8 49.9 1.0 N A:ASP69 4.8 51.2 1.0 CA A:VAL111 4.9 56.1 1.0 CA A:LEU68 4.9 49.8 1.0 C A:THR110 4.9 55.5 1.0 CG A:ASP69 5.0 55.5 1.0 CB A:VAL111 5.0 55.9 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