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Copper in PDB 7ev7: Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K

Enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K

All present enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K:
7.1.1.9;

Protein crystallography data

The structure of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K, PDB code: 7ev7 was solved by A.Shimada, S.Yoshikawa, T.Tsukihara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.74 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 181.539, 203.655, 177.569, 90, 90, 90
R / Rfree (%) 15.9 / 17.8

Other elements in 7ev7:

The structure of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K also contains other interesting chemical elements:

Zinc (Zn) 2 atoms
Magnesium (Mg) 2 atoms
Sodium (Na) 4 atoms
Iron (Fe) 4 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K (pdb code 7ev7). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K, PDB code: 7ev7:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 7ev7

Go back to Copper Binding Sites List in 7ev7
Copper binding site 1 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu604

b:20.9
occ:1.00
C A:CMO607 1.9 16.2 0.6
NE2 A:HIS291 2.0 20.5 1.0
NE2 A:HIS290 2.1 20.3 1.0
ND1 A:HIS240 2.1 19.9 1.0
O A:CMO607 2.2 16.2 0.1
CE1 A:HIS291 2.9 19.7 1.0
O A:CMO607 2.9 17.0 0.6
CE1 A:HIS240 3.0 24.1 1.0
CD2 A:HIS291 3.1 20.2 1.0
CE1 A:HIS290 3.1 19.9 1.0
CD2 A:HIS290 3.1 21.3 1.0
CG A:HIS240 3.2 19.7 1.0
C A:CMO607 3.3 16.2 0.1
CB A:HIS240 3.6 21.4 1.0
ND1 A:HIS291 4.0 19.3 1.0
CG A:HIS291 4.1 17.3 1.0
NE2 A:HIS240 4.2 20.0 1.0
CA A:HIS240 4.2 19.5 1.0
ND1 A:HIS290 4.2 18.9 1.0
CG A:HIS290 4.2 20.8 1.0
NA A:HEA603 4.3 20.1 1.0
CD2 A:HIS240 4.3 21.2 1.0
C1A A:HEA603 4.3 20.4 1.0
C4A A:HEA603 4.4 19.0 1.0
C2A A:HEA603 4.6 19.8 1.0
C3A A:HEA603 4.6 20.8 1.0
CG2 A:VAL243 4.7 20.4 1.0
CHA A:HEA603 4.8 19.2 1.0
FE A:HEA603 4.9 20.9 1.0

Copper binding site 2 out of 6 in 7ev7

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Copper binding site 2 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu304

b:21.6
occ:1.00
CU1 B:CUA304 0.0 21.6 1.0
ND1 B:HIS161 2.1 26.8 1.0
SG B:CYS196 2.3 24.9 1.0
SD B:MET207 2.4 22.5 1.0
SG B:CYS200 2.4 22.2 1.0
CU2 B:CUA304 2.4 21.6 1.0
CE1 B:HIS161 3.0 25.1 1.0
CE B:MET207 3.2 25.1 1.0
CG B:HIS161 3.2 22.1 1.0
CB B:CYS200 3.3 19.9 1.0
CG B:MET207 3.4 20.1 1.0
CB B:CYS196 3.4 23.5 1.0
CB B:HIS161 3.6 19.2 1.0
NE2 B:HIS161 4.2 22.6 1.0
O B:GLU198 4.2 21.1 1.0
CA B:HIS161 4.2 20.7 1.0
CD2 B:HIS161 4.3 22.4 1.0
ND1 B:HIS204 4.4 23.9 1.0
CD1 B:TRP104 4.5 21.9 1.0
O B:HIS102 4.7 23.7 1.0
CA B:CYS200 4.7 22.4 1.0
CA B:HIS204 4.7 23.3 1.0
O B:LEU160 4.8 23.0 1.0
CA B:CYS196 4.8 21.6 1.0
CB B:MET207 4.9 23.9 1.0

Copper binding site 3 out of 6 in 7ev7

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Copper binding site 3 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu304

b:21.6
occ:1.00
CU2 B:CUA304 0.0 21.6 1.0
ND1 B:HIS204 2.0 23.9 1.0
SG B:CYS200 2.3 22.2 1.0
SG B:CYS196 2.3 24.9 1.0
CU1 B:CUA304 2.4 21.6 1.0
O B:GLU198 2.7 21.1 1.0
CE1 B:HIS204 2.9 21.9 1.0
CG B:HIS204 3.1 20.8 1.0
CB B:CYS196 3.3 23.5 1.0
CB B:CYS200 3.3 19.9 1.0
CA B:HIS204 3.6 23.3 1.0
CB B:HIS204 3.6 19.8 1.0
C B:GLU198 3.7 20.4 1.0
N B:CYS200 3.7 23.4 1.0
O B:HIS204 3.9 24.2 1.0
NE2 B:HIS204 4.1 22.0 1.0
ND1 B:HIS161 4.1 26.8 1.0
CA B:CYS200 4.1 22.4 1.0
CD2 B:HIS204 4.2 22.0 1.0
C B:HIS204 4.2 24.2 1.0
C B:CYS196 4.2 20.4 1.0
N B:GLU198 4.2 21.5 1.0
O B:CYS196 4.2 22.8 1.0
CA B:ILE199 4.3 21.5 1.0
C B:ILE199 4.3 24.7 1.0
SD B:MET207 4.3 22.5 1.0
CA B:CYS196 4.4 21.6 1.0
N B:ILE199 4.4 20.8 1.0
CG B:MET207 4.5 20.1 1.0
N B:SER197 4.6 19.8 1.0
CA B:GLU198 4.6 22.0 1.0
N B:HIS204 4.8 22.6 1.0
CA B:HIS161 4.9 20.7 1.0
CB B:HIS161 5.0 19.2 1.0

Copper binding site 4 out of 6 in 7ev7

Go back to Copper Binding Sites List in 7ev7
Copper binding site 4 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Cu604

b:23.6
occ:1.00
C N:CMO607 1.9 19.6 0.6
NE2 N:HIS290 2.1 22.7 1.0
NE2 N:HIS291 2.1 23.0 1.0
ND1 N:HIS240 2.1 19.7 1.0
O N:CMO607 2.2 18.0 0.2
CE1 N:HIS291 2.9 22.7 1.0
O N:CMO607 2.9 19.7 0.6
CE1 N:HIS240 3.0 23.1 1.0
CD2 N:HIS290 3.0 22.6 1.0
CE1 N:HIS290 3.1 24.2 1.0
CD2 N:HIS291 3.1 24.0 1.0
CG N:HIS240 3.2 19.7 1.0
C N:CMO607 3.4 19.4 0.2
CB N:HIS240 3.6 21.8 1.0
ND1 N:HIS291 4.0 20.7 1.0
CG N:HIS291 4.1 20.7 1.0
NE2 N:HIS240 4.1 20.6 1.0
CA N:HIS240 4.1 21.6 1.0
ND1 N:HIS290 4.2 21.3 1.0
CG N:HIS290 4.2 21.1 1.0
CD2 N:HIS240 4.3 19.6 1.0
NA N:HEA603 4.3 23.2 1.0
C1A N:HEA603 4.3 24.3 1.0
C4A N:HEA603 4.4 20.8 1.0
C2A N:HEA603 4.6 22.8 1.0
C3A N:HEA603 4.6 23.4 1.0
CHA N:HEA603 4.8 21.7 1.0
CG2 N:VAL243 4.8 23.3 1.0
FE N:HEA603 4.9 23.4 1.0

Copper binding site 5 out of 6 in 7ev7

Go back to Copper Binding Sites List in 7ev7
Copper binding site 5 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu302

b:25.6
occ:1.00
CU1 O:CUA302 0.0 25.6 1.0
ND1 O:HIS161 2.1 28.5 1.0
SD O:MET207 2.3 27.6 1.0
SG O:CYS196 2.4 29.4 1.0
SG O:CYS200 2.4 28.8 1.0
CU2 O:CUA302 2.5 25.9 1.0
CE1 O:HIS161 3.0 27.2 1.0
CE O:MET207 3.2 29.1 1.0
CG O:HIS161 3.2 27.7 1.0
CB O:CYS200 3.3 25.2 1.0
CG O:MET207 3.4 25.1 1.0
CB O:CYS196 3.5 28.6 1.0
CB O:HIS161 3.6 27.3 1.0
NE2 O:HIS161 4.1 27.5 1.0
O O:GLU198 4.2 24.5 1.0
CA O:HIS161 4.2 26.8 1.0
CD2 O:HIS161 4.3 26.5 1.0
ND1 O:HIS204 4.4 28.1 1.0
CD1 O:TRP104 4.5 29.7 1.0
O O:HIS102 4.7 28.7 1.0
CA O:CYS200 4.7 26.9 1.0
CA O:HIS204 4.7 28.9 1.0
O O:LEU160 4.7 27.6 1.0
CA O:CYS196 4.8 27.6 1.0
CB O:MET207 4.9 27.8 1.0
N O:CYS200 5.0 26.9 1.0

Copper binding site 6 out of 6 in 7ev7

Go back to Copper Binding Sites List in 7ev7
Copper binding site 6 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at A 50 K within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu302

b:25.9
occ:1.00
CU2 O:CUA302 0.0 25.9 1.0
ND1 O:HIS204 2.0 28.1 1.0
SG O:CYS196 2.3 29.4 1.0
SG O:CYS200 2.3 28.8 1.0
CU1 O:CUA302 2.5 25.6 1.0
O O:GLU198 2.6 24.5 1.0
CE1 O:HIS204 2.9 25.9 1.0
CG O:HIS204 3.1 26.6 1.0
CB O:CYS196 3.3 28.6 1.0
CB O:CYS200 3.4 25.2 1.0
CA O:HIS204 3.5 28.9 1.0
CB O:HIS204 3.6 28.1 1.0
N O:CYS200 3.7 26.9 1.0
C O:GLU198 3.7 22.8 1.0
O O:HIS204 3.9 28.7 1.0
NE2 O:HIS204 4.0 26.5 1.0
C O:HIS204 4.2 27.2 1.0
ND1 O:HIS161 4.2 28.5 1.0
CA O:CYS200 4.2 26.9 1.0
CD2 O:HIS204 4.2 26.2 1.0
C O:CYS196 4.2 27.6 1.0
O O:CYS196 4.2 27.6 1.0
N O:GLU198 4.2 27.1 1.0
CA O:ILE199 4.3 25.0 1.0
C O:ILE199 4.3 27.3 1.0
SD O:MET207 4.3 27.6 1.0
CA O:CYS196 4.3 27.6 1.0
N O:ILE199 4.4 23.7 1.0
CG O:MET207 4.5 25.1 1.0
N O:SER197 4.6 26.1 1.0
CA O:GLU198 4.6 26.0 1.0
N O:HIS204 4.7 27.4 1.0
CA O:HIS161 4.9 26.8 1.0

Reference:

A.Shimada, K.Shinzawa-Itoh, K.Muramoto, T.Tsukihara, S.Yoshikawa. Structure of Co-Bound Fully Reduced State of Bovine Heart Cytochrome C Oxidase To Be Published.
Page generated: Mon Jul 14 08:00:44 2025

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