Magnesium in PDB 3bhv: Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Variolin B

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

The structure of Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Variolin B, PDB code: 3bhv 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 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.160, 133.968, 147.879, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 22.9

The binding sites of Magnesium atom in the Structure of Phosphorylated THR160 CDK2/Cyclin A in Complex with the Inhibitor Variolin B (pdb code 3bhv). 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 Variolin B, PDB code: 3bhv:
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 Variolin B


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 Variolin B within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1 b:38.3 occ:1.00 O B:HOH613 2.2 35.2 1.0 O B:GLN203 2.4 37.0 1.0 O B:ILE206 2.4 36.4 1.0 O B:MET200 2.6 39.9 1.0 O B:HOH648 2.7 34.8 1.0 C B:GLN203 3.5 37.4 1.0 C B:ILE206 3.6 36.3 1.0 C B:MET200 3.8 39.9 1.0 CB B:GLN203 4.0 36.6 1.0 CA B:GLN203 4.2 37.1 1.0 CG B:MET200 4.3 39.0 1.0 N B:GLN203 4.3 38.3 1.0 N B:ILE206 4.4 37.4 1.0 CA B:THR207 4.4 34.5 1.0 N B:THR207 4.4 35.4 1.0 CA B:ILE206 4.6 36.9 1.0 CG2 B:THR207 4.6 34.6 1.0 N B:PRO204 4.6 37.6 1.0 CA B:MET200 4.7 39.1 1.0 N B:LYS201 4.7 40.9 1.0 SD B:MET200 4.7 40.0 1.0 C B:PRO204 4.7 38.0 1.0 O B:HOH439 4.7 31.8 1.0 CA B:LYS201 4.8 42.2 1.0 C B:LYS201 4.8 42.0 1.0 O B:PRO204 4.8 38.1 1.0 O B:LYS201 4.9 42.5 1.0 CA B:PRO204 4.9 37.9 1.0 N B:ASP205 4.9 37.9 1.0 CB B:MET200 4.9 39.6 1.0

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


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 Variolin B within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg2 b:31.1 occ:1.00 O D:GLN203 2.1 36.0 1.0 O D:ILE206 2.4 34.5 1.0 O D:MET200 2.5 37.1 1.0 O D:HOH658 2.5 45.8 1.0 O D:HOH650 2.6 27.4 1.0 O D:HOH682 2.8 45.2 1.0 C D:GLN203 3.2 35.9 1.0 C D:ILE206 3.7 34.7 1.0 C D:MET200 3.7 37.5 1.0 CB D:GLN203 3.9 35.1 1.0 CA D:GLN203 3.9 35.5 1.0 N D:GLN203 4.1 36.6 1.0 O D:HOH636 4.1 54.8 1.0 CG D:MET200 4.2 39.1 1.0 N D:PRO204 4.3 36.5 1.0 N D:ILE206 4.3 35.5 1.0 C D:PRO204 4.5 37.1 1.0 CA D:PRO204 4.5 36.9 1.0 N D:THR207 4.5 34.1 1.0 CA D:MET200 4.6 37.7 1.0 CA D:THR207 4.6 33.7 1.0 CA D:ILE206 4.6 34.9 1.0 CG2 D:THR207 4.6 33.6 1.0 N D:LYS201 4.6 37.5 1.0 CA D:LYS201 4.7 38.2 1.0 O D:PRO204 4.7 37.0 1.0 C D:LYS201 4.7 37.9 1.0 SD D:MET200 4.8 40.4 1.0 N D:ASP205 4.8 37.2 1.0 O D:HOH631 4.8 32.7 1.0 CB D:MET200 4.9 38.2 1.0 O D:LYS201 4.9 37.8 1.0 O D:HOH648 5.0 36.5 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