Copper in PDB 7au6: Cytochrome C Oxidase Structure in O-State

All present enzymatic activity of Cytochrome C Oxidase Structure in O-State:
7.1.1.9;

The structure of Cytochrome C Oxidase Structure in O-State also contains other interesting chemical elements:

Manganese	(Mn)	1 atom
Calcium	(Ca)	1 atom
Iron	(Fe)	2 atoms

The binding sites of Copper atom in the Cytochrome C Oxidase Structure in O-State (pdb code 7au6). 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 Structure in O-State, PDB code: 7au6:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Cytochrome C Oxidase Structure in O-State


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 Structure in O-State within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu603 b:15.8 occ:1.00 O2 A:PEO611 2.0 8.4 1.0 ND1 A:HIS276 2.2 6.8 1.0 NE2 A:HIS325 2.2 8.5 1.0 NE2 A:HIS326 2.3 7.4 1.0 O1 A:PEO611 2.5 8.4 1.0 CD2 A:HIS326 3.0 7.4 1.0 CE1 A:HIS325 3.1 8.5 1.0 CE1 A:HIS276 3.1 6.8 1.0 CE1 A:HIS326 3.2 7.4 1.0 CG A:HIS276 3.3 6.8 1.0 CD2 A:HIS325 3.3 8.5 1.0 CB A:HIS276 3.6 6.8 1.0 O2 A:OXY605 3.7 8.4 1.0 CA A:HIS276 4.0 6.8 1.0 CG A:HIS326 4.1 7.4 1.0 ND1 A:HIS326 4.2 7.4 1.0 ND1 A:HIS325 4.3 8.5 1.0 NE2 A:HIS276 4.3 6.8 1.0 NA A:HEA602 4.3 8.8 1.0 CG A:HIS325 4.4 8.5 1.0 CD2 A:HIS276 4.4 6.8 1.0 C1A A:HEA602 4.4 8.8 1.0 O1 A:OXY605 4.4 8.4 1.0 C4A A:HEA602 4.6 8.8 1.0 FE A:HEA602 4.7 8.8 1.0 CHA A:HEA602 4.8 8.8 1.0 C2A A:HEA602 4.8 8.8 1.0 C3A A:HEA602 4.9 8.8 1.0 ND A:HEA602 4.9 8.8 1.0 N A:HIS276 4.9 6.8 1.0 C4D A:HEA602 5.0 8.8 1.0

Copper binding site 2 out of 3 in the Cytochrome C Oxidase Structure in O-State


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 Structure in O-State within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:8.2 occ:1.00 CU1 B:CUA301 0.0 8.2 1.0 ND1 B:HIS224 2.3 6.5 1.0 O B:GLU218 2.4 7.7 1.0 CU2 B:CUA301 2.6 8.2 1.0 SG B:CYS216 2.8 7.2 1.0 CB B:CYS220 2.9 7.1 1.0 CE1 B:HIS224 3.0 6.5 1.0 SG B:CYS220 3.0 7.1 1.0 C B:GLU218 3.4 7.7 1.0 N B:CYS220 3.5 7.1 1.0 CB B:CYS216 3.5 7.2 1.0 CG B:HIS224 3.6 6.5 1.0 CA B:CYS220 3.8 7.1 1.0 CA B:HIS224 4.0 6.5 1.0 O B:HIS224 4.0 6.5 1.0 C B:LEU219 4.0 7.2 1.0 N B:GLU218 4.1 7.7 1.0 CB B:HIS224 4.1 6.5 1.0 CA B:LEU219 4.2 7.2 1.0 N B:LEU219 4.2 7.2 1.0 NE2 B:HIS224 4.2 6.5 1.0 CA B:GLU218 4.3 7.7 1.0 C B:CYS216 4.4 7.2 1.0 O B:CYS216 4.4 7.2 1.0 C B:HIS224 4.4 6.5 1.0 CD2 B:HIS224 4.5 6.5 1.0 SD B:MET227 4.5 7.0 1.0 CA B:CYS216 4.6 7.2 1.0 N B:SER217 4.7 7.3 1.0 ND1 B:HIS181 4.8 6.8 1.0 O B:LEU219 4.9 7.2 1.0 CA B:HIS181 4.9 6.8 1.0 C B:CYS220 4.9 7.1 1.0 CG B:MET227 4.9 7.0 1.0 O B:ILE180 5.0 7.2 1.0

Copper binding site 3 out of 3 in the Cytochrome C Oxidase Structure in O-State


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 Structure in O-State within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:8.2 occ:1.00 CU2 B:CUA301 0.0 8.2 1.0 ND1 B:HIS181 2.6 6.8 1.0 SD B:MET227 2.6 7.0 1.0 CU1 B:CUA301 2.6 8.2 1.0 SG B:CYS220 2.7 7.1 1.0 SG B:CYS216 2.9 7.2 1.0 CB B:CYS220 2.9 7.1 1.0 CE B:MET227 3.0 7.0 1.0 CE1 B:HIS181 3.5 6.8 1.0 CG B:HIS181 3.5 6.8 1.0 CB B:HIS181 3.7 6.8 1.0 CG B:MET227 3.8 7.0 1.0 CB B:CYS216 3.8 7.2 1.0 CA B:HIS181 4.2 6.8 1.0 O B:GLU218 4.3 7.7 1.0 CA B:CYS220 4.4 7.1 1.0 NE2 B:HIS181 4.6 6.8 1.0 CD2 B:HIS181 4.7 6.8 1.0 ND1 B:HIS224 4.8 6.5 1.0 N B:TRP121 4.8 6.3 1.0 O B:ILE180 4.8 7.2 1.0 O B:HIS119 4.9 7.1 1.0 CD1 B:TRP121 4.9 6.3 1.0 O B:HIS224 4.9 6.5 1.0 N B:CYS220 4.9 7.1 1.0

F.Kolbe, S.Safarian, H.Michel. Cytochrome C Oxidase Structure in O-State To Be Published.