Magnesium in PDB 3bht: Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Meriolin 3

All present enzymatic activity of Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Meriolin 3:
2.7.11.22;

The structure of Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Meriolin 3, PDB code: 3bht was solved by A.Echalier, K.Bettayeb, Y.Ferandin, O.Lozach, M.Clement, A.Valette, F.Liger, B.Marquet, J.C.Morris, J.A.Endicott, B.Joseph, L.Meijer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.128, 133.770, 147.831, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 22

The binding sites of Magnesium atom in the Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Meriolin 3 (pdb code 3bht). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Meriolin 3, PDB code: 3bht:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Meriolin 3


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Meriolin 3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1 b:15.1 occ:1.00 O B:GLN203 2.3 7.0 1.0 O B:HOH640 2.4 13.6 1.0 O B:ILE206 2.5 5.5 1.0 O B:MET200 2.6 10.4 1.0 O B:HOH669 2.7 19.9 1.0 C B:GLN203 3.5 7.5 1.0 C B:ILE206 3.7 5.8 1.0 C B:MET200 3.7 10.3 1.0 CB B:GLN203 4.0 7.4 1.0 CA B:GLN203 4.1 7.5 1.0 CG B:MET200 4.2 10.2 1.0 N B:GLN203 4.3 8.7 1.0 N B:ILE206 4.4 6.4 1.0 CA B:THR207 4.5 5.1 1.0 N B:PRO204 4.5 7.5 1.0 N B:THR207 4.6 5.0 1.0 N B:LYS201 4.6 10.8 1.0 CA B:MET200 4.6 9.9 1.0 C B:PRO204 4.6 7.5 1.0 CA B:LYS201 4.7 11.6 1.0 CA B:ILE206 4.7 5.8 1.0 SD B:MET200 4.7 11.1 1.0 CG2 B:THR207 4.8 5.3 1.0 C B:LYS201 4.8 11.2 1.0 O B:PRO204 4.8 7.3 1.0 CA B:PRO204 4.8 7.7 1.0 O B:LYS201 4.9 11.4 1.0 CB B:MET200 4.9 10.1 1.0 N B:ASP205 4.9 7.4 1.0 O B:HOH440 4.9 9.4 1.0

Magnesium binding site 2 out of 2 in the Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Meriolin 3


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Meriolin 3 within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg2 b:9.9 occ:1.00 O D:GLN203 2.1 3.1 1.0 O D:HOH623 2.3 18.4 1.0 O D:HOH615 2.5 8.8 1.0 O D:MET200 2.5 7.3 1.0 O D:ILE206 2.5 2.0 1.0 O D:HOH647 2.7 22.5 1.0 C D:GLN203 3.3 3.5 1.0 C D:MET200 3.7 7.8 1.0 C D:ILE206 3.8 3.4 1.0 O D:HOH601 4.0 30.2 1.0 CB D:GLN203 4.0 2.9 1.0 CA D:GLN203 4.0 3.5 1.0 N D:GLN203 4.1 4.9 1.0 CG D:MET200 4.3 9.4 1.0 N D:PRO204 4.4 3.4 1.0 N D:ILE206 4.4 4.0 1.0 O D:HOH672 4.5 27.0 1.0 CA D:PRO204 4.6 3.6 1.0 CG2 D:THR207 4.6 2.9 1.0 N D:LYS201 4.6 7.4 1.0 CA D:THR207 4.6 2.9 1.0 CA D:MET200 4.6 8.3 1.0 C D:PRO204 4.6 3.6 1.0 N D:THR207 4.6 3.1 1.0 C D:LYS201 4.6 6.8 1.0 CA D:LYS201 4.6 7.5 1.0 O D:LYS201 4.6 6.6 1.0 CA D:ILE206 4.7 3.5 1.0 O D:HOH597 4.8 12.6 1.0 SD D:MET200 4.8 11.7 1.0 O D:HOH613 4.9 19.7 1.0 O D:PRO204 4.9 3.4 1.0 CB D:MET200 4.9 8.7 1.0 N D:ASP205 4.9 3.7 1.0

K.Bettayeb, O.M.Tirado, S.Marionneau-Lambot, Y.Ferandin, O.Lozach, J.C.Morris, S.Mateo-Lozano, P.Drueckes, M.H.Kubbutat, F.Liger, B.Marquet, B.Joseph, A.Echalier, J.A.Endicott, V.Notario, L.Meijer. Meriolins, A New Class of Cell Death Inducing Kinase Inhibitors with Enhanced Selectivity For Cyclin-Dependent Kinases Cancer Res. V. 67 8325 2007.
ISSN: ISSN 0008-5472
PubMed: 17804748
DOI: 10.1158/0008-5472.CAN-07-1826