Magnesium in PDB 1hck: Human Cyclin-Dependent Kinase 2

All present enzymatic activity of Human Cyclin-Dependent Kinase 2:
2.7.1.37;

The structure of Human Cyclin-Dependent Kinase 2, PDB code: 1hck was solved by U.Schulze-Gahmen, H.L.De Bondt, S.-H.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	72.820, 72.660, 54.070, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 27.2

The binding sites of Magnesium atom in the Human Cyclin-Dependent Kinase 2 (pdb code 1hck). 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 Human Cyclin-Dependent Kinase 2, PDB code: 1hck:

Magnesium binding site 1 out of 1 in the Human Cyclin-Dependent Kinase 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Cyclin-Dependent Kinase 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:32.4 occ:0.60 O1A A:ATP400 1.8 34.5 1.0 O1G A:ATP400 1.9 61.4 1.0 O2B A:ATP400 2.0 58.1 1.0 OD2 A:ASP145 2.1 31.9 1.0 OD1 A:ASN132 2.2 35.5 1.0 O A:HOH503 2.3 38.5 1.0 PA A:ATP400 3.0 45.5 1.0 PB A:ATP400 3.1 53.2 1.0 PG A:ATP400 3.2 56.6 1.0 CG A:ASP145 3.3 26.7 1.0 O3A A:ATP400 3.3 50.7 1.0 O3B A:ATP400 3.3 54.0 1.0 CG A:ASN132 3.4 31.7 1.0 O5' A:ATP400 3.7 43.5 1.0 O2G A:ATP400 3.8 57.4 1.0 NZ A:LYS33 4.0 52.3 1.0 OD1 A:ASP145 4.0 26.1 1.0 ND2 A:ASN132 4.0 38.0 1.0 CB A:ASP145 4.1 21.9 1.0 O2A A:ATP400 4.2 42.5 1.0 O3G A:ATP400 4.3 57.6 1.0 O1B A:ATP400 4.4 55.0 1.0 O A:GLN131 4.4 28.0 1.0 CA A:ASN132 4.5 22.3 1.0 CB A:ASN132 4.5 28.1 1.0 CE A:LYS129 4.8 27.3 1.0 C8 A:ATP400 4.9 19.3 1.0 C A:GLN131 4.9 23.5 1.0 N A:ASN132 4.9 23.3 1.0 C2' A:ATP400 5.0 38.9 1.0 O A:HOH502 5.0 45.2 1.0

U.Schulze-Gahmen, H.L.De Bondt, S.H.Kim. High-Resolution Crystal Structures of Human Cyclin-Dependent Kinase 2 with and Without Atp: Bound Waters and Natural Ligand As Guides For Inhibitor Design. J.Med.Chem. V. 39 4540 1996.
ISSN: ISSN 0022-2623
PubMed: 8917641
DOI: 10.1021/JM960402A