Zinc in PDB 4md8: Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E)

All present enzymatic activity of Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E):
2.7.11.1;

The structure of Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E), PDB code: 4md8 was solved by G.Lolli, A.Ranchio, R.Battistutta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	181.21 / 3.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	141.518, 57.625, 185.685, 90.00, 102.60, 90.00
R / Rfree (%)	22.2 / 24.9

The binding sites of Zinc atom in the Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E) (pdb code 4md8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E), PDB code: 4md8:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E)


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 Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:29.4 occ:1.00 SG A:CYS109 2.2 40.1 1.0 SG A:CYS114 2.2 35.0 1.0 SG A:CYS140 2.2 30.4 1.0 SG A:CYS137 2.3 30.1 1.0 CB A:CYS137 3.2 28.0 1.0 CB A:CYS114 3.2 34.0 1.0 CB A:CYS140 3.2 32.8 1.0 CB A:CYS109 3.3 36.7 1.0 N A:CYS140 3.7 33.7 1.0 CA A:CYS140 4.1 34.3 1.0 OH A:TYR144 4.1 31.5 1.0 CB A:ARG111 4.1 48.9 1.0 NH1 A:ARG111 4.2 53.6 1.0 CE1 A:TYR144 4.2 30.0 1.0 CD A:ARG111 4.4 54.8 1.0 CA A:CYS114 4.6 36.0 1.0 CZ A:TYR144 4.6 30.3 1.0 CA A:CYS137 4.6 27.9 1.0 CA A:CYS109 4.7 36.7 1.0 CB A:LYS139 4.7 38.1 1.0 CG A:ARG111 4.7 53.0 1.0 C A:LYS139 4.8 35.1 1.0 C A:CYS140 5.0 33.6 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E)


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 Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:33.0 occ:1.00 SG B:CYS114 2.1 33.0 1.0 SG B:CYS109 2.2 31.6 1.0 SG B:CYS140 2.2 37.0 1.0 SG B:CYS137 2.3 43.6 1.0 CB B:CYS137 3.1 41.1 1.0 CB B:CYS114 3.1 35.0 1.0 CB B:CYS140 3.2 39.1 1.0 CB B:CYS109 3.3 33.1 1.0 N B:CYS140 3.6 43.5 1.0 CA B:CYS140 4.0 42.0 1.0 OH B:TYR144 4.1 35.2 1.0 NH1 B:ARG111 4.2 32.8 1.0 CE1 B:TYR144 4.2 35.7 1.0 CB B:ARG111 4.3 29.2 1.0 CD B:ARG111 4.4 29.7 1.0 CA B:CYS137 4.6 41.3 1.0 CZ B:TYR144 4.6 35.6 1.0 CB B:LYS139 4.6 45.0 1.0 CA B:CYS114 4.6 36.1 1.0 C B:LYS139 4.7 46.5 1.0 CA B:CYS109 4.7 33.0 1.0 CG B:ARG111 4.8 28.8 1.0 C B:CYS140 4.9 41.8 1.0 C B:CYS137 4.9 42.2 1.0 N B:LYS139 5.0 47.5 1.0 CA B:LYS139 5.0 46.9 1.0 O B:CYS137 5.0 42.0 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E) within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn301 b:47.3 occ:1.00 SG C:CYS140 2.2 46.0 1.0 SG C:CYS109 2.2 48.9 1.0 SG C:CYS137 2.3 48.1 1.0 SG C:CYS114 2.3 45.0 1.0 CB C:CYS137 3.0 49.3 1.0 CB C:CYS140 3.2 49.3 1.0 CB C:CYS109 3.3 46.5 1.0 CB C:CYS114 3.4 48.3 1.0 N C:CYS140 3.7 52.7 1.0 OH C:TYR144 4.0 45.8 1.0 CA C:CYS140 4.0 52.0 1.0 CE1 C:TYR144 4.1 43.9 1.0 CB C:ARG111 4.2 48.9 1.0 NH1 C:ARG111 4.4 49.0 1.0 CZ C:TYR144 4.4 44.5 1.0 CA C:CYS137 4.5 48.1 1.0 CD C:ARG111 4.5 47.5 1.0 CA C:CYS109 4.7 46.2 1.0 CB C:LYS139 4.7 52.5 1.0 CA C:CYS114 4.8 51.9 1.0 C C:LYS139 4.8 52.4 1.0 CG C:ARG111 4.8 48.1 1.0 C C:CYS140 4.9 52.2 1.0 C C:CYS137 4.9 47.7 1.0 O C:CYS137 4.9 47.8 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Full-Length Symmetric CK2 Holoenzyme with Mutated Alpha Subunit (F121E) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn301 b:40.8 occ:1.00 SG D:CYS109 2.1 48.7 1.0 SG D:CYS114 2.2 46.2 1.0 SG D:CYS137 2.3 55.5 1.0 SG D:CYS140 2.3 52.6 1.0 CB D:CYS137 3.1 52.1 1.0 CB D:CYS109 3.1 48.7 1.0 CB D:CYS114 3.1 48.9 1.0 CB D:CYS140 3.3 54.9 1.0 N D:CYS140 3.8 56.1 1.0 CA D:CYS140 4.1 56.2 1.0 CB D:ARG111 4.1 50.8 1.0 OH D:TYR144 4.2 53.8 1.0 CE1 D:TYR144 4.2 52.0 1.0 NH1 D:ARG111 4.3 52.0 1.0 CD D:ARG111 4.5 50.6 1.0 CA D:CYS109 4.5 47.4 1.0 CA D:CYS114 4.6 51.5 1.0 CA D:CYS137 4.6 51.2 1.0 CZ D:TYR144 4.6 52.1 1.0 CB D:LYS139 4.7 58.8 1.0 CG D:ARG111 4.8 50.1 1.0 C D:LYS139 4.9 58.2 1.0

G.Lolli, A.Ranchio, R.Battistutta. Active Form of the Protein Kinase CK2 Alpha 2 Beta 2 Holoenzyme Is A Strong Complex with Symmetric Architecture. Acs Chem.Biol. V. 9 366 2014.
ISSN: ISSN 1554-8929
PubMed: 24175891
DOI: 10.1021/CB400771Y