Copper in PDB 8f6c: E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer

All present enzymatic activity of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer:
7.1.1.3;

The structure of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Copper atom in the E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer (pdb code 8f6c). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer, PDB code: 8f6c:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1003 b:29.6 occ:1.00 NE2 A:HIS334 2.0 29.6 1.0 ND1 A:HIS284 2.1 28.9 1.0 NE2 A:HIS333 2.1 29.7 1.0 CE1 A:HIS284 2.5 28.9 1.0 CE1 A:HIS334 2.5 29.6 1.0 CE1 A:HIS333 2.5 29.7 1.0 CD2 A:HIS334 3.0 29.6 1.0 CG A:HIS284 3.1 28.8 1.0 CHA A:HEO1002 3.3 29.5 1.0 CD2 A:HIS333 3.3 29.7 1.0 C1A A:HEO1002 3.4 29.5 1.0 ND1 A:HIS334 3.5 29.6 1.0 NE2 A:HIS284 3.5 28.9 1.0 ND1 A:HIS333 3.7 29.7 1.0 CG A:HIS334 3.8 29.6 1.0 CD2 A:HIS284 3.8 28.8 1.0 CB A:HIS284 3.8 28.8 1.0 C2A A:HEO1002 3.9 29.5 1.0 NA A:HEO1002 3.9 29.5 1.0 C4D A:HEO1002 4.0 29.5 1.0 CG A:HIS333 4.1 29.7 1.0 CAA A:HEO1002 4.3 29.5 1.0 ND A:HEO1002 4.4 29.5 1.0 CA A:HIS284 4.5 28.8 1.0 C3A A:HEO1002 4.6 29.5 1.0 C4A A:HEO1002 4.7 29.5 1.0 NB A:HEO1002 4.8 29.5 1.0 C3D A:HEO1002 4.9 29.5 1.0

Copper binding site 2 out of 2 in the E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of E. Coli Cytochrome BO3 Ubiquinol Oxidase Dimer within 5.0Å range: probe atom residue distance (Å) B Occ E:Cu1003 b:29.6 occ:1.00 NE2 E:HIS334 2.0 29.6 1.0 ND1 E:HIS284 2.1 28.8 1.0 NE2 E:HIS333 2.1 29.7 1.0 CE1 E:HIS284 2.5 28.9 1.0 CE1 E:HIS334 2.5 29.6 1.0 CE1 E:HIS333 2.5 29.7 1.0 CD2 E:HIS334 3.0 29.6 1.0 CG E:HIS284 3.1 28.8 1.0 CHA E:HEO1002 3.3 29.5 1.0 CD2 E:HIS333 3.3 29.7 1.0 C1A E:HEO1002 3.4 29.5 1.0 ND1 E:HIS334 3.5 29.6 1.0 NE2 E:HIS284 3.5 28.8 1.0 ND1 E:HIS333 3.7 29.7 1.0 CG E:HIS334 3.8 29.6 1.0 CD2 E:HIS284 3.8 28.8 1.0 CB E:HIS284 3.8 28.8 1.0 C2A E:HEO1002 3.9 29.5 1.0 NA E:HEO1002 3.9 29.5 1.0 C4D E:HEO1002 4.0 29.5 1.0 CG E:HIS333 4.1 29.7 1.0 CAA E:HEO1002 4.3 29.5 1.0 ND E:HEO1002 4.4 29.5 1.0 CA E:HIS284 4.5 28.8 1.0 C3A E:HEO1002 4.6 29.5 1.0 C4A E:HEO1002 4.7 29.5 1.0 NB E:HEO1002 4.8 29.5 1.0 C3D E:HEO1002 4.9 29.5 1.0

Y.Guo, E.Karimullina, D.Borek, A.Savchenko. Monomer and Dimer Structures of E. Coli Cytochrome BO3 Ubiquinol Oxidase To Be Published.