Copper in PDB 7au3: Cytochrome C Oxidase Structure in F-State

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

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

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

The binding sites of Copper atom in the Cytochrome C Oxidase Structure in F-State (pdb code 7au3). 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 F-State, PDB code: 7au3:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Cytochrome C Oxidase Structure in F-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 F-State within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu604 b:12.0 occ:1.00 NE2 A:HIS325 2.1 4.5 1.0 NE2 A:HIS326 2.2 3.9 1.0 ND1 A:HIS276 2.3 3.8 1.0 CE1 A:HIS325 2.8 4.5 1.0 CE1 A:HIS276 2.9 3.8 1.0 O A:O606 3.0 5.0 1.0 CE1 A:HIS326 3.1 3.9 1.0 CD2 A:HIS326 3.2 3.9 1.0 CD2 A:HIS325 3.2 4.5 1.0 O1 A:2FK607 3.3 5.5 1.0 CG A:HIS276 3.4 3.8 1.0 O2 A:2FK607 3.9 5.5 1.0 CB A:HIS276 4.0 3.8 1.0 ND1 A:HIS325 4.0 4.5 1.0 NE2 A:HIS276 4.1 3.8 1.0 ND1 A:HIS326 4.1 3.9 1.0 NA A:HEA603 4.1 5.3 1.0 CG A:HIS326 4.2 3.9 1.0 CG A:HIS325 4.2 4.5 1.0 C1A A:HEA603 4.3 5.3 1.0 CD2 A:HIS276 4.4 3.8 1.0 C4A A:HEA603 4.5 5.3 1.0 FE A:HEA603 4.5 5.3 1.0 CA A:HIS276 4.5 3.8 1.0 O A:HOH787 4.5 5.4 1.0 ND A:HEA603 4.7 5.3 1.0 CHA A:HEA603 4.7 5.3 1.0 CG2 A:VAL279 4.7 3.8 1.0 C4D A:HEA603 4.7 5.3 1.0 C2A A:HEA603 4.8 5.3 1.0 C3A A:HEA603 4.8 5.3 1.0 NB A:HEA603 4.9 5.3 1.0 CHB A:HEA603 5.0 5.3 1.0

Copper binding site 2 out of 3 in the Cytochrome C Oxidase Structure in F-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 F-State within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:15.4 occ:1.00 CU1 B:CUA301 0.0 15.4 1.0 ND1 B:HIS224 1.8 4.9 1.0 SG B:CYS220 2.6 5.1 1.0 CE1 B:HIS224 2.6 4.9 1.0 SG B:CYS216 2.6 5.0 1.0 O B:GLU218 2.7 5.2 1.0 CU2 B:CUA301 2.7 15.4 1.0 CG B:HIS224 3.0 4.9 1.0 CB B:CYS216 3.2 5.0 1.0 O B:HIS224 3.5 4.9 1.0 CA B:HIS224 3.5 4.9 1.0 CB B:HIS224 3.6 4.9 1.0 CB B:CYS220 3.6 5.1 1.0 C B:GLU218 3.7 5.2 1.0 NE2 B:HIS224 3.8 4.9 1.0 N B:CYS220 3.8 5.1 1.0 C B:HIS224 3.9 4.9 1.0 CD2 B:HIS224 4.0 4.9 1.0 C B:CYS216 4.1 5.0 1.0 O B:CYS216 4.1 5.0 1.0 CA B:CYS216 4.2 5.0 1.0 N B:GLU218 4.2 5.2 1.0 CA B:CYS220 4.3 5.1 1.0 SD B:MET227 4.3 4.6 1.0 C B:LEU219 4.4 5.0 1.0 CA B:LEU219 4.4 5.0 1.0 ND1 B:HIS181 4.5 4.6 1.0 N B:LEU219 4.5 5.0 1.0 CG B:MET227 4.6 4.6 1.0 N B:SER217 4.6 4.9 1.0 CA B:GLU218 4.6 5.2 1.0 N B:HIS224 4.9 4.9 1.0

Copper binding site 3 out of 3 in the Cytochrome C Oxidase Structure in F-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 F-State within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:15.4 occ:1.00 CU2 B:CUA301 0.0 15.4 1.0 ND1 B:HIS181 2.0 4.6 1.0 SG B:CYS220 2.3 5.1 1.0 SD B:MET227 2.5 4.6 1.0 SG B:CYS216 2.6 5.0 1.0 CU1 B:CUA301 2.7 15.4 1.0 CE1 B:HIS181 2.8 4.6 1.0 CB B:CYS220 3.1 5.1 1.0 CG B:HIS181 3.2 4.6 1.0 CE B:MET227 3.3 4.6 1.0 CB B:HIS181 3.7 4.6 1.0 CB B:CYS216 3.7 5.0 1.0 CG B:MET227 3.8 4.6 1.0 NE2 B:HIS181 4.0 4.6 1.0 CD2 B:HIS181 4.2 4.6 1.0 CA B:HIS181 4.2 4.6 1.0 O B:GLU218 4.2 5.2 1.0 ND1 B:HIS224 4.4 4.9 1.0 CA B:CYS220 4.5 5.1 1.0 CD1 B:TRP121 4.7 4.3 1.0 N B:CYS220 4.8 5.1 1.0 CA B:HIS224 4.9 4.9 1.0 O B:HIS119 4.9 4.1 1.0 O B:ILE180 4.9 4.4 1.0 O B:HIS224 5.0 4.9 1.0

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