Copper in PDB 7ate: Cytochrome C Oxidase Structure in P-State

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

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

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

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

Copper binding site 1 out of 3 in the Cytochrome C Oxidase Structure in P-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 P-State within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu604 b:22.1 occ:1.00 NE2 A:HIS325 2.0 10.8 1.0 NE2 A:HIS326 2.2 10.1 1.0 O1 A:PEO606 2.3 12.9 1.0 ND1 A:HIS276 2.3 8.7 1.0 O2 A:PEO606 2.6 12.9 1.0 CE1 A:HIS326 2.7 10.1 1.0 CE1 A:HIS325 2.7 10.8 1.0 CE1 A:HIS276 3.1 8.7 1.0 CD2 A:HIS325 3.2 10.8 1.0 CD2 A:HIS326 3.2 10.1 1.0 CG A:HIS276 3.3 8.7 1.0 CB A:HIS276 3.6 8.7 1.0 ND1 A:HIS326 3.8 10.1 1.0 ND1 A:HIS325 3.9 10.8 1.0 CA A:HIS276 4.1 8.7 1.0 CG A:HIS326 4.1 10.1 1.0 CG A:HIS325 4.2 10.8 1.0 NE2 A:HIS276 4.2 8.7 1.0 NA A:HEA603 4.2 12.8 1.0 CD2 A:HIS276 4.3 8.7 1.0 O A:HOH737 4.4 12.6 1.0 O A:HOH768 4.4 11.9 1.0 C1A A:HEA603 4.4 12.8 1.0 C4A A:HEA603 4.5 12.8 1.0 FE A:HEA603 4.7 12.8 1.0 CG2 A:VAL279 4.8 9.0 1.0 C2A A:HEA603 4.8 12.8 1.0 CHA A:HEA603 4.8 12.8 1.0 C3A A:HEA603 4.8 12.8 1.0 ND A:HEA603 4.9 12.8 1.0 N A:HIS276 4.9 8.7 1.0 C4D A:HEA603 5.0 12.8 1.0 CHB A:HEA603 5.0 12.8 1.0

Copper binding site 2 out of 3 in the Cytochrome C Oxidase Structure in P-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 P-State within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:20.9 occ:1.00 CU1 B:CUA301 0.0 20.9 1.0 ND1 B:HIS224 2.3 9.8 1.0 O B:GLU218 2.3 11.3 1.0 SG B:CYS216 2.6 10.4 1.0 SG B:CYS220 2.7 10.2 1.0 CU2 B:CUA301 2.7 20.9 1.0 CE1 B:HIS224 2.9 9.8 1.0 CB B:CYS220 3.2 10.2 1.0 CB B:CYS216 3.3 10.4 1.0 C B:GLU218 3.4 11.3 1.0 CG B:HIS224 3.5 9.8 1.0 N B:CYS220 3.6 10.2 1.0 O B:HIS224 3.9 9.8 1.0 N B:GLU218 4.0 11.3 1.0 O B:CYS216 4.0 10.4 1.0 CA B:HIS224 4.0 9.8 1.0 C B:CYS216 4.0 10.4 1.0 CA B:CYS220 4.0 10.2 1.0 CB B:HIS224 4.1 9.8 1.0 NE2 B:HIS224 4.1 9.8 1.0 N B:LEU219 4.2 10.2 1.0 C B:LEU219 4.2 10.2 1.0 CA B:LEU219 4.2 10.2 1.0 CA B:CYS216 4.3 10.4 1.0 CA B:GLU218 4.3 11.3 1.0 C B:HIS224 4.4 9.8 1.0 CD2 B:HIS224 4.4 9.8 1.0 N B:SER217 4.5 11.2 1.0 ND1 B:HIS181 4.7 10.1 1.0 SD B:MET227 4.7 10.2 1.0 CG B:MET227 4.9 10.2 1.0 CA B:HIS181 5.0 10.1 1.0 C B:SER217 5.0 11.2 1.0

Copper binding site 3 out of 3 in the Cytochrome C Oxidase Structure in P-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 P-State within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:20.9 occ:1.00 CU2 B:CUA301 0.0 20.9 1.0 ND1 B:HIS181 2.3 10.1 1.0 SG B:CYS220 2.5 10.2 1.0 SD B:MET227 2.6 10.2 1.0 SG B:CYS216 2.6 10.4 1.0 CU1 B:CUA301 2.7 20.9 1.0 CB B:CYS220 2.9 10.2 1.0 CE1 B:HIS181 3.2 10.1 1.0 CG B:HIS181 3.3 10.1 1.0 CE B:MET227 3.3 10.2 1.0 CB B:HIS181 3.6 10.1 1.0 CB B:CYS216 3.6 10.4 1.0 CG B:MET227 3.7 10.2 1.0 O B:GLU218 4.2 11.3 1.0 CA B:HIS181 4.2 10.1 1.0 NE2 B:HIS181 4.4 10.1 1.0 CA B:CYS220 4.4 10.2 1.0 CD2 B:HIS181 4.4 10.1 1.0 CD1 B:TRP121 4.7 9.8 1.0 ND1 B:HIS224 4.8 9.8 1.0 N B:CYS220 4.8 10.2 1.0 O B:HIS119 5.0 9.9 1.0 N B:TRP121 5.0 9.8 1.0

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