Magnesium in PDB 8fp5: CDK2 Liganded with Atp and MG2+

All present enzymatic activity of CDK2 Liganded with Atp and MG2+:
2.7.11.22;

The structure of CDK2 Liganded with Atp and MG2+, PDB code: 8fp5 was solved by E.Schonbrunn, L.Sun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.60 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.67, 71.71, 72.04, 90, 90, 90
R / Rfree (%)	19.4 / 23

The binding sites of Magnesium atom in the CDK2 Liganded with Atp and MG2+ (pdb code 8fp5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the CDK2 Liganded with Atp and MG2+, PDB code: 8fp5:

Magnesium binding site 1 out of 1 in the CDK2 Liganded with Atp and MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of CDK2 Liganded with Atp and MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:27.1 occ:0.85 OD2 A:ASP145 2.1 30.9 1.0 O2G A:ATP302 2.1 29.7 1.0 O1B A:ATP302 2.2 29.9 1.0 OD1 A:ASN132 2.2 25.6 1.0 O2A A:ATP302 2.2 27.5 1.0 O A:HOH497 2.3 25.1 1.0 PB A:ATP302 3.1 33.0 1.0 CG A:ASN132 3.3 24.5 1.0 PG A:ATP302 3.3 33.9 1.0 PA A:ATP302 3.3 31.2 1.0 CG A:ASP145 3.3 30.2 1.0 O3B A:ATP302 3.4 32.1 1.0 O3A A:ATP302 3.5 27.6 1.0 ND2 A:ASN132 3.8 24.2 1.0 NZ A:LYS33 3.9 28.8 1.0 O5' A:ATP302 4.0 31.2 1.0 O3G A:ATP302 4.0 36.8 1.0 CB A:ASP145 4.2 28.1 1.0 OD1 A:ASP145 4.2 33.5 1.0 O A:GLN131 4.4 24.2 1.0 CB A:ASN132 4.5 20.1 1.0 O1G A:ATP302 4.5 35.3 1.0 CA A:ASN132 4.5 20.5 1.0 O1A A:ATP302 4.5 33.0 1.0 O2B A:ATP302 4.5 36.5 1.0 C A:GLN131 4.8 22.5 1.0 N A:ASN132 4.9 20.2 1.0 C8 A:ATP302 4.9 30.0 1.0 O A:HOH458 4.9 34.1 1.0 C2' A:ATP302 4.9 35.6 1.0

E.Schonbrunn, L.Sun. Development of Allosteric, Selective Cyclin-Dependent Kinase 2 (CDK2) Inhibitors That Are Negatively Cooperative with Cyclin Binding and Show Potential As Contraceptive Agents To Be Published.