Copper in PDB 6ymy: Cytochrome C Oxidase From Saccharomyces Cerevisiae

All present enzymatic activity of Cytochrome C Oxidase From Saccharomyces Cerevisiae:
1.9.3.1;

The structure of Cytochrome C Oxidase From Saccharomyces Cerevisiae also contains other interesting chemical elements:

Zinc	(Zn)	1 atom
Iron	(Fe)	2 atoms

The binding sites of Copper atom in the Cytochrome C Oxidase From Saccharomyces Cerevisiae (pdb code 6ymy). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Cytochrome C Oxidase From Saccharomyces Cerevisiae, PDB code: 6ymy:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Cytochrome C Oxidase From Saccharomyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cytochrome C Oxidase From Saccharomyces Cerevisiae within 5.0Å range: probe atom residue distance (Å) B Occ a:Cu601 b:0.2 occ:1.00 ND1 a:HIS241 2.1 98.4 1.0 NE2 a:HIS291 2.1 0.2 1.0 NE2 a:HIS290 2.2 0.2 1.0 CE1 a:HIS291 2.4 0.2 1.0 CE1 a:HIS241 2.8 98.4 1.0 CD2 a:HIS290 3.1 0.2 1.0 CE1 a:HIS290 3.1 0.2 1.0 CG a:HIS241 3.3 98.4 1.0 CD2 a:HIS291 3.3 0.2 1.0 ND1 a:HIS291 3.6 0.2 1.0 C1A a:HEA603 3.7 98.5 1.0 NA a:HEA603 3.7 98.5 1.0 CB a:HIS241 3.9 98.4 1.0 CHA a:HEA603 3.9 98.5 1.0 CG a:HIS291 4.0 0.2 1.0 NE2 a:HIS241 4.1 98.4 1.0 C4D a:HEA603 4.1 98.5 1.0 FE a:HEA603 4.2 98.5 1.0 ND a:HEA603 4.2 98.5 1.0 ND1 a:HIS290 4.2 0.2 1.0 CG a:HIS290 4.2 0.2 1.0 C4A a:HEA603 4.3 98.5 1.0 CD2 a:HIS241 4.3 98.4 1.0 C2A a:HEA603 4.3 98.5 1.0 CA a:HIS241 4.5 98.4 1.0 C3A a:HEA603 4.6 98.5 1.0 NB a:HEA603 4.8 98.5 1.0 CG1 a:VAL244 4.9 98.3 1.0 C3D a:HEA603 4.9 98.5 1.0 CHB a:HEA603 5.0 98.5 1.0 CG2 a:VAL244 5.0 98.3 1.0

Copper binding site 2 out of 3 in the Cytochrome C Oxidase From Saccharomyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cytochrome C Oxidase From Saccharomyces Cerevisiae within 5.0Å range: probe atom residue distance (Å) B Occ b:Cu301 b:0.7 occ:1.00 CU1 b:CUA301 0.0 0.7 1.0 CU2 b:CUA301 2.7 0.7 1.0 ND1 b:HIS229 2.8 0.4 1.0 O b:GLU223 2.8 0.5 1.0 SG b:CYS221 3.0 99.9 1.0 CB b:CYS225 3.2 0.9 1.0 SG b:CYS225 3.2 0.9 1.0 O b:HIS229 3.4 0.4 1.0 N b:CYS225 3.5 0.9 1.0 CA b:HIS229 3.5 0.4 1.0 CG b:HIS229 3.6 0.4 1.0 CB b:HIS186 3.6 0.6 1.0 CB b:HIS229 3.7 0.4 1.0 CE1 b:HIS229 3.8 0.4 1.0 C b:HIS229 3.9 0.4 1.0 CA b:CYS225 4.0 0.9 1.0 C b:GLU223 4.0 0.5 1.0 CB b:CYS221 4.1 99.9 1.0 C b:LEU224 4.1 0.6 1.0 CG b:HIS186 4.3 0.6 1.0 CA b:LEU224 4.4 0.6 1.0 SD b:MET232 4.4 99.7 1.0 CE b:MET232 4.6 99.7 1.0 N b:LEU224 4.7 0.6 1.0 CD2 b:HIS229 4.8 0.4 1.0 N b:HIS229 4.8 0.4 1.0 CG b:MET232 4.8 99.7 1.0 O b:CYS221 4.8 99.9 1.0 CA b:HIS186 4.8 0.6 1.0 NE2 b:HIS229 4.8 0.4 1.0 O b:GLY228 4.9 0.7 1.0 ND1 b:HIS186 4.9 0.6 1.0 O b:LEU224 5.0 0.6 1.0 CD2 b:HIS186 5.0 0.6 1.0 C b:CYS221 5.0 99.9 1.0

Copper binding site 3 out of 3 in the Cytochrome C Oxidase From Saccharomyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Cytochrome C Oxidase From Saccharomyces Cerevisiae within 5.0Å range: probe atom residue distance (Å) B Occ b:Cu301 b:0.7 occ:1.00 CU2 b:CUA301 0.0 0.7 1.0 CG b:HIS186 2.5 0.6 1.0 CE b:MET232 2.6 99.7 1.0 CU1 b:CUA301 2.7 0.7 1.0 CD2 b:HIS186 2.8 0.6 1.0 SD b:MET232 2.8 99.7 1.0 ND1 b:HIS186 2.8 0.6 1.0 CB b:HIS186 2.9 0.6 1.0 NE2 b:HIS186 3.3 0.6 1.0 CE1 b:HIS186 3.3 0.6 1.0 SG b:CYS221 3.4 99.9 1.0 CB b:CYS225 3.5 0.9 1.0 SG b:CYS225 3.6 0.9 1.0 CG b:MET232 4.0 99.7 1.0 O b:GLN123 4.1 0.1 1.0 CA b:HIS186 4.4 0.6 1.0 CB b:CYS221 4.4 99.9 1.0 C b:GLN123 4.5 0.1 1.0 CA b:GLN123 4.8 0.1 1.0 O b:GLU223 4.8 0.5 1.0 CA b:CYS225 4.9 0.9 1.0 C b:HIS186 4.9 0.6 1.0

J.Berndtsson, A.Aufschnaiter, S.Rathore, L.Marin-Buera, H.Dawitz, J.Diessl, V.Kohler, A.Barrientos, S.Buttner, F.Fontanesi, M.Ott. Mitochondrial Respiratory Supercomplex Formation Improves Bioenergetics and Confers A Selectable Fitness Advantage To Be Published.