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Magnesium in PDB 7vuw: Bovine Heart Cytochrome C Oxidase in the Cyanide-Bound Fully Oxidized State at 50 K

Enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Cyanide-Bound Fully Oxidized State at 50 K

All present enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Cyanide-Bound Fully Oxidized State at 50 K:
7.1.1.9;

Protein crystallography data

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

Resolution Low / High (Å) 39.92 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 182.076, 204.481, 177.68, 90, 90, 90
R / Rfree (%) 15.4 / 17.5

Other elements in 7vuw:

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

Copper (Cu) 6 atoms
Zinc (Zn) 2 atoms
Iron (Fe) 4 atoms
Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Bovine Heart Cytochrome C Oxidase in the Cyanide-Bound Fully Oxidized State at 50 K (pdb code 7vuw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Bovine Heart Cytochrome C Oxidase in the Cyanide-Bound Fully Oxidized State at 50 K, PDB code: 7vuw:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7vuw

Go back to Magnesium Binding Sites List in 7vuw
Magnesium binding site 1 out of 2 in the Bovine Heart Cytochrome C Oxidase in the Cyanide-Bound Fully Oxidized State at 50 K


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bovine Heart Cytochrome C Oxidase in the Cyanide-Bound Fully Oxidized State at 50 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg604

b:20.8
occ:1.00
OD2 A:ASP369 2.0 21.5 1.0
O B:HOH482 2.1 19.5 1.0
OE1 B:GLU198 2.1 24.1 1.0
O A:HOH881 2.1 20.0 1.0
O B:HOH461 2.1 21.0 1.0
NE2 A:HIS368 2.2 19.9 1.0
CD B:GLU198 3.1 21.6 1.0
CE1 A:HIS368 3.1 20.4 1.0
CD2 A:HIS368 3.2 20.6 1.0
CG A:ASP369 3.2 20.7 1.0
OE2 B:GLU198 3.4 22.3 1.0
O B:SER197 3.9 20.8 1.0
CB A:ASP369 3.9 21.7 1.0
O A:HOH891 4.0 21.7 1.0
OD1 A:ASP369 4.2 22.6 1.0
ND1 A:HIS368 4.3 19.0 1.0
OD1 B:ASP173 4.3 21.7 1.0
CG A:HIS368 4.3 20.0 1.0
O A:HOH774 4.3 20.5 1.0
OD2 B:ASP173 4.3 21.1 1.0
O B:HOH507 4.4 23.5 0.4
OG1 A:THR294 4.4 21.6 1.0
CG B:GLU198 4.4 19.6 1.0
O B:HOH540 4.5 19.8 0.6
O A:HOH883 4.5 20.4 1.0
O A:HOH724 4.5 20.2 1.0
O A:HOH822 4.6 22.0 1.0
CB B:GLU198 4.6 21.0 1.0
CG B:ASP173 4.7 20.5 1.0
CA B:GLU198 4.9 21.6 1.0

Magnesium binding site 2 out of 2 in 7vuw

Go back to Magnesium Binding Sites List in 7vuw
Magnesium binding site 2 out of 2 in the Bovine Heart Cytochrome C Oxidase in the Cyanide-Bound Fully Oxidized State at 50 K


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Bovine Heart Cytochrome C Oxidase in the Cyanide-Bound Fully Oxidized State at 50 K within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Mg604

b:25.2
occ:1.00
OD2 N:ASP369 2.1 24.2 1.0
OE1 O:GLU198 2.1 31.5 1.0
O O:HOH474 2.1 25.5 1.0
O O:HOH534 2.1 25.5 1.0
O O:HOH441 2.1 25.3 1.0
NE2 N:HIS368 2.2 23.9 1.0
CD O:GLU198 3.1 25.5 1.0
CD2 N:HIS368 3.1 24.9 1.0
CE1 N:HIS368 3.2 25.2 1.0
CG N:ASP369 3.3 25.0 1.0
OE2 O:GLU198 3.4 27.7 1.0
O O:SER197 3.9 27.5 1.0
CB N:ASP369 4.0 27.3 1.0
O N:HOH896 4.0 25.3 1.0
OD1 N:ASP369 4.2 27.0 1.0
O N:HOH807 4.3 23.4 1.0
ND1 N:HIS368 4.3 23.0 1.0
CG N:HIS368 4.3 23.3 1.0
OD1 O:ASP173 4.3 26.4 1.0
OD2 O:ASP173 4.3 26.6 1.0
CG O:GLU198 4.4 25.4 1.0
O O:HOH468 4.4 26.9 0.4
OG1 N:THR294 4.4 26.0 1.0
O N:HOH711 4.5 23.7 1.0
O O:HOH541 4.5 25.9 0.6
O N:HOH881 4.5 23.3 1.0
O N:HOH850 4.6 26.2 1.0
CB O:GLU198 4.6 26.0 1.0
CG O:ASP173 4.7 27.0 1.0
CA O:GLU198 4.9 26.8 1.0

Reference:

A.Shimada, T.Tsukihara. Bovine Cytochrome C Oxidese in Cn-Bound Fully Oxidized State at 50 K To Be Published.
Page generated: Thu Aug 14 17:16:29 2025

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