Magnesium in PDB 3nsz: Human CK2 Catalytic Domain in Complex with Amppn

All present enzymatic activity of Human CK2 Catalytic Domain in Complex with Amppn:
2.7.11.1;

The structure of Human CK2 Catalytic Domain in Complex with Amppn, PDB code: 3nsz was solved by A.D.Ferguson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.382, 62.026, 117.061, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 18.7

The binding sites of Magnesium atom in the Human CK2 Catalytic Domain in Complex with Amppn (pdb code 3nsz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human CK2 Catalytic Domain in Complex with Amppn, PDB code: 3nsz:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Human CK2 Catalytic Domain in Complex with Amppn


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human CK2 Catalytic Domain in Complex with Amppn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg900 b:26.9 occ:1.00 O1A A:ANP1000 2.6 13.2 1.0 O3' A:ANP1000 2.6 15.9 1.0 OD1 A:ASN161 2.7 11.1 1.0 O A:HOH395 2.8 18.5 1.0 O A:HOH477 3.1 21.1 1.0 CD2 A:HIS160 3.2 18.1 0.4 C3' A:ANP1000 3.3 15.0 1.0 OD2 A:ASP175 3.6 12.4 1.0 O A:HIS160 3.7 12.5 1.0 NE2 A:HIS160 3.7 18.0 0.4 PA A:ANP1000 3.8 12.1 1.0 CB A:ASP175 3.9 9.8 1.0 C5' A:ANP1000 3.9 13.8 1.0 CG A:ASN161 3.9 10.2 1.0 CD1 A:ILE174 3.9 13.0 1.0 O5' A:ANP1000 4.0 12.8 1.0 CG A:ASP175 4.0 11.6 1.0 C4' A:ANP1000 4.1 14.1 1.0 CG A:HIS160 4.4 16.2 0.4 C A:HIS160 4.4 12.0 1.0 CA A:ASN161 4.6 9.2 1.0 C2' A:ANP1000 4.6 14.8 1.0 O A:HOH429 4.7 19.2 1.0 CG1 A:ILE174 4.7 9.5 1.0 ND2 A:ASN161 4.7 10.3 1.0 O3A A:ANP1000 4.7 12.4 1.0 CB A:ASN161 4.8 9.5 1.0 N A:ASN161 4.8 9.0 1.0 N3B A:ANP1000 4.8 12.4 1.0 CE1 A:HIS160 5.0 17.9 0.4 O2A A:ANP1000 5.0 12.3 1.0

Magnesium binding site 2 out of 2 in the Human CK2 Catalytic Domain in Complex with Amppn


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human CK2 Catalytic Domain in Complex with Amppn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg901 b:23.2 occ:1.00 OD2 A:ASP175 2.6 12.4 1.0 N3B A:ANP1000 2.6 12.4 1.0 O A:HOH441 2.9 22.5 1.0 OD1 A:ASP175 3.2 12.2 1.0 O A:HOH570 3.3 31.2 1.0 CG A:ASP175 3.3 11.6 1.0 O A:HOH395 3.5 18.5 1.0 O1B A:ANP1000 3.7 14.3 1.0 CB A:LYS49 3.7 19.9 1.0 O A:HOH394 3.8 14.8 1.0 PB A:ANP1000 3.8 13.0 1.0 O A:HOH477 4.0 21.1 1.0 OD2 A:ASP156 4.3 11.9 1.0 O1A A:ANP1000 4.4 13.2 1.0 CD A:LYS49 4.4 48.0 1.0 N A:LYS49 4.5 17.4 1.0 CG A:LYS49 4.7 38.2 1.0 CB A:ASP175 4.7 9.8 1.0 CA A:LYS49 4.8 17.5 1.0 O3A A:ANP1000 4.9 12.4 1.0 O2B A:ANP1000 4.9 13.6 1.0

A.D.Ferguson, P.R.Sheth, A.D.Basso, S.Paliwal, K.Gray, T.O.Fischmann, H.V.Le. Structural Basis of Cx-4945 Binding to Human Protein Kinase CK2. Febs Lett. V. 585 104 2011.
ISSN: ISSN 0014-5793
PubMed: 21093442
DOI: 10.1016/J.FEBSLET.2010.11.019