Copper in PDB 2e47: 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: 2e47 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 structure of Crystal Structure Analysis of the Clock Protein EA4 (Glycosylation Form) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Copper atom in the Crystal Structure Analysis of the Clock Protein EA4 (Glycosylation Form) (pdb code 2e47). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure Analysis of the Clock Protein EA4 (Glycosylation Form), PDB code: 2e47:
Jump to Copper binding site number: 1; 2;

Copper 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 Copper with other atoms in the Cu 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:Cu171 b:52.7 occ:1.00 ND1 A:HIS50 2.0 22.3 1.0 NE2 A:HIS67 2.0 25.6 1.0 NE2 A:HIS52 2.1 26.9 1.0 NE2 A:HIS124 2.1 27.7 1.0 CE1 A:HIS124 2.7 22.6 1.0 CD2 A:HIS67 2.7 20.9 1.0 CE1 A:HIS52 2.8 21.3 1.0 CE1 A:HIS50 2.9 24.1 1.0 CG A:HIS50 3.1 20.2 1.0 O A:HOH1049 3.1 38.4 1.0 CD2 A:HIS52 3.2 18.2 1.0 O A:HOH1023 3.2 30.6 1.0 CE1 A:HIS67 3.3 24.6 1.0 CD2 A:HIS124 3.3 19.7 1.0 CB A:HIS50 3.6 18.2 1.0 ND1 A:HIS124 3.9 20.4 1.0 ND1 A:HIS52 3.9 22.4 1.0 CG A:HIS67 4.0 22.6 1.0 NE2 A:HIS50 4.1 19.1 1.0 CG A:HIS124 4.2 19.2 1.0 CG A:HIS52 4.2 18.0 1.0 CD2 A:HIS50 4.2 20.3 1.0 ND1 A:HIS67 4.2 16.8 1.0 O A:HOH1019 4.7 28.8 1.0 O A:HOH1063 4.8 44.6 1.0 CA A:HIS50 4.8 18.6 1.0 CB A:VAL122 4.9 16.4 1.0 N A:HIS50 5.0 18.4 1.0

Copper 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 Copper with other atoms in the Cu 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:Cu171 b:56.7 occ:1.00 ND1 B:HIS50 2.1 29.0 1.0 NE2 B:HIS124 2.1 32.7 1.0 NE2 B:HIS67 2.1 30.4 1.0 NE2 B:HIS52 2.1 29.5 1.0 CE1 B:HIS124 2.5 28.4 1.0 CD2 B:HIS67 2.7 25.9 1.0 CE1 B:HIS52 2.8 20.6 1.0 CE1 B:HIS50 2.8 27.2 1.0 O B:HOH2019 3.1 32.6 1.0 CG B:HIS50 3.2 24.4 1.0 CD2 B:HIS52 3.2 21.2 1.0 CD2 B:HIS124 3.3 22.9 1.0 CE1 B:HIS67 3.3 25.5 1.0 CB B:HIS50 3.7 23.7 1.0 ND1 B:HIS124 3.7 23.5 1.0 CG B:HIS67 4.0 25.6 1.0 ND1 B:HIS52 4.0 25.0 1.0 NE2 B:HIS50 4.1 28.3 1.0 CG B:HIS124 4.1 24.8 1.0 CG B:HIS52 4.2 23.1 1.0 CD2 B:HIS50 4.2 24.8 1.0 ND1 B:HIS67 4.2 26.5 1.0 O B:HOH2028 4.7 35.7 1.0 CB B:VAL122 4.9 20.9 1.0 CA B:HIS50 4.9 23.0 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.