Zinc in PDB 4dgl: Crystal Structure of the CK2 Tetrameric Holoenzyme

All present enzymatic activity of Crystal Structure of the CK2 Tetrameric Holoenzyme:
2.7.11.1;

The structure of Crystal Structure of the CK2 Tetrameric Holoenzyme, PDB code: 4dgl was solved by G.Lolli, R.Battistutta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	152.12 / 3.00
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	175.652, 175.652, 96.260, 90.00, 90.00, 120.00
R / Rfree (%)	19.5 / 22.2

The binding sites of Zinc atom in the Crystal Structure of the CK2 Tetrameric Holoenzyme (pdb code 4dgl). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the CK2 Tetrameric Holoenzyme, PDB code: 4dgl:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the CK2 Tetrameric Holoenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the CK2 Tetrameric Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:76.0 occ:1.00 SG A:CYS109 2.2 79.8 1.0 SG A:CYS140 2.2 80.0 1.0 SG A:CYS114 2.3 73.0 1.0 SG A:CYS137 2.5 83.4 1.0 CB A:CYS114 3.1 78.2 1.0 CB A:CYS140 3.2 77.8 1.0 CB A:CYS137 3.3 82.2 1.0 CB A:CYS109 3.4 86.0 1.0 N A:CYS140 3.7 84.2 1.0 CB A:ARG111 3.9 79.3 1.0 CA A:CYS140 4.1 81.3 1.0 NH1 A:ARG111 4.2 77.0 1.0 OH A:TYR144 4.2 79.9 1.0 CD A:ARG111 4.3 74.0 1.0 CE1 A:TYR144 4.4 76.0 1.0 CA A:CYS114 4.6 82.2 1.0 CZ A:TYR144 4.6 77.0 1.0 CB A:LYS139 4.7 80.8 1.0 CG A:ARG111 4.7 77.1 1.0 CA A:CYS137 4.7 82.0 1.0 CA A:CYS109 4.8 87.2 1.0 CE A:MET119 4.8 86.8 1.0 C A:LYS139 4.9 83.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the CK2 Tetrameric Holoenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the CK2 Tetrameric Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:73.3 occ:1.00 SG B:CYS114 2.2 78.8 1.0 SG B:CYS109 2.3 76.8 1.0 SG B:CYS140 2.3 71.1 1.0 SG B:CYS137 2.4 78.8 1.0 CB B:CYS140 3.1 68.5 1.0 CB B:CYS137 3.2 74.0 1.0 CB B:CYS114 3.3 77.0 1.0 CB B:CYS109 3.4 82.5 1.0 N B:CYS140 3.7 76.0 1.0 CA B:CYS140 4.0 75.1 1.0 OH B:TYR144 4.0 86.2 1.0 NH1 B:ARG111 4.1 81.0 1.0 CE1 B:TYR144 4.3 80.3 1.0 CB B:ARG111 4.4 76.6 1.0 CA B:CYS137 4.6 74.4 1.0 CZ B:TYR144 4.6 84.2 1.0 CD B:ARG111 4.6 76.1 1.0 CB B:LYS139 4.7 75.7 1.0 CA B:CYS114 4.7 77.8 1.0 CA B:CYS109 4.8 82.0 1.0 O B:CYS137 4.8 76.5 1.0 C B:LYS139 4.8 75.5 1.0 C B:CYS140 4.9 76.0 1.0 C B:CYS137 4.9 76.1 1.0 CG B:ARG111 4.9 77.1 1.0

G.Lolli, L.A.Pinna, R.Battistutta. Structural Determinants of Protein Kinase CK2 Regulation By Autoinhibitory Polymerization. Acs Chem.Biol. V. 7 1158 2012.
ISSN: ISSN 1554-8929
PubMed: 22506723
DOI: 10.1021/CB300054N