Zinc in PDB 6ffz: Crystal Structure Analysis of the Clock Protein EA4 (Glycosylation Form)

The structure of Crystal Structure Analysis of the Clock Protein EA4 (Glycosylation Form), PDB code: 6ffz was solved by S.-Y.Park, T.Hiraki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.11
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.098, 73.894, 47.446, 90.00, 104.07, 90.00
R / Rfree (%)	17 / 25.1

The binding sites of Zinc atom in the Crystal Structure Analysis of the Clock Protein EA4 (Glycosylation Form) (pdb code 6ffz). 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 Analysis of the Clock Protein EA4 (Glycosylation Form), PDB code: 6ffz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure Analysis of the Clock Protein EA4 (Glycosylation Form)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of the Clock Protein EA4 (Glycosylation Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn172 b:24.3 occ:1.00 ND1 A:HIS67 2.0 16.8 1.0 ND1 A:HIS75 2.1 22.7 1.0 OD1 A:ASP87 2.1 20.1 1.0 ND1 A:HIS84 2.1 23.8 1.0 CE1 A:HIS84 2.9 25.5 1.0 CE1 A:HIS75 2.9 23.6 1.0 CG A:ASP87 3.0 23.6 1.0 CG A:HIS67 3.0 22.6 1.0 CE1 A:HIS67 3.1 24.6 1.0 CG A:HIS75 3.2 21.7 1.0 OD2 A:ASP87 3.2 22.5 1.0 CG A:HIS84 3.2 26.5 1.0 CB A:HIS67 3.3 23.2 1.0 CB A:HIS75 3.6 24.4 1.0 CB A:HIS84 3.7 22.4 1.0 O A:LYS140 3.8 31.0 1.0 CA A:HIS75 3.9 25.6 1.0 NE2 A:HIS84 4.1 28.0 1.0 NE2 A:HIS75 4.1 24.6 1.0 CD2 A:HIS67 4.2 20.9 1.0 NE2 A:HIS67 4.2 25.6 1.0 CD2 A:HIS84 4.2 26.0 1.0 CD2 A:HIS75 4.2 21.9 1.0 CB A:ASP87 4.4 20.3 1.0 O A:HOH1014 4.5 26.4 1.0 C A:LYS140 4.7 32.0 1.0 CA A:ASP87 4.8 21.9 1.0 N A:HIS84 4.8 22.7 1.0 CA A:HIS67 4.9 23.0 1.0 N A:HIS75 4.9 25.6 1.0 N A:GLY76 4.9 25.5 1.0 CA A:HIS84 4.9 22.6 1.0 C A:HIS75 4.9 25.7 1.0 CA A:THR141 5.0 29.5 1.0 N A:ASP87 5.0 21.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure Analysis of the Clock Protein EA4 (Glycosylation Form)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure Analysis of the Clock Protein EA4 (Glycosylation Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn172 b:25.8 occ:1.00 OD1 B:ASP87 2.1 23.2 1.0 ND1 B:HIS84 2.1 21.2 1.0 ND1 B:HIS75 2.1 20.8 1.0 ND1 B:HIS67 2.1 26.5 1.0 CE1 B:HIS75 2.8 24.3 1.0 CE1 B:HIS84 2.9 18.0 1.0 CG B:HIS67 3.0 25.6 1.0 CG B:ASP87 3.0 27.9 1.0 CG B:HIS84 3.2 21.9 1.0 CE1 B:HIS67 3.2 25.5 1.0 CB B:HIS67 3.2 22.9 1.0 CG B:HIS75 3.3 29.2 1.0 OD2 B:ASP87 3.4 28.0 1.0 CB B:HIS84 3.7 23.2 1.0 O B:LYS140 3.7 39.0 1.0 CB B:HIS75 3.8 30.0 1.0 NE2 B:HIS75 4.0 25.5 1.0 NE2 B:HIS84 4.1 21.4 1.0 CA B:HIS75 4.1 31.2 1.0 CD2 B:HIS67 4.2 25.9 1.0 CD2 B:HIS84 4.2 19.3 1.0 NE2 B:HIS67 4.2 30.4 1.0 CD2 B:HIS75 4.3 27.1 1.0 CB B:ASP87 4.4 25.3 1.0 C B:LYS140 4.8 39.6 1.0 CA B:HIS67 4.8 24.2 1.0 CA B:ASP87 4.8 26.1 1.0 N B:HIS84 4.8 24.6 1.0 CA B:HIS84 4.9 23.3 1.0 N B:GLY76 5.0 29.7 1.0

T.Hiraki, N.Shibayama, J.R.M.Tame, S.Akashi, S.-Y.Park. The Clock Protein EA4 Ticks Away with Movement of A Mobile Copper Ion To Be Published.