Magnesium in PDB 3asn: Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength

All present enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength:
1.9.3.1;

The structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength, PDB code: 3asn was solved by M.Suga, N.Yano, K.Muramoto, K.Shinzawa-Itoh, T.Maeda, E.Yamashita, T.Tsukihara, S.Yoshikawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	181.826, 204.098, 177.829, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 18.7

The structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength also contains other interesting chemical elements:

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

The binding sites of Magnesium atom in the Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength (pdb code 3asn). 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 Fully Oxidized State Measured at 1.7470 Angstrom Wavelength, PDB code: 3asn:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength


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 Fully Oxidized State Measured at 1.7470 Angstrom Wavelength within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg518 b:15.1 occ:1.00 NE2 A:HIS368 2.0 17.4 1.0 OD1 A:ASP369 2.1 18.7 1.0 OE1 B:GLU198 2.1 17.6 1.0 O A:HOH2267 2.4 17.3 1.0 O B:HOH2268 2.4 16.1 1.0 O B:HOH2266 2.4 13.7 1.0 CE1 A:HIS368 2.9 13.0 1.0 CD2 A:HIS368 3.0 13.7 1.0 CD B:GLU198 3.2 19.7 1.0 CG A:ASP369 3.3 18.2 1.0 OE2 B:GLU198 3.7 22.1 1.0 O B:SER197 3.9 15.3 1.0 O A:HOH2278 4.0 8.8 1.0 CB A:ASP369 4.0 15.9 1.0 ND1 A:HIS368 4.1 10.1 1.0 CG A:HIS368 4.1 13.8 1.0 OD1 B:ASP173 4.2 13.5 1.0 OD2 B:ASP173 4.3 18.4 1.0 OD2 A:ASP369 4.3 18.6 1.0 O A:HOH2297 4.3 11.3 1.0 OG1 A:THR294 4.4 18.1 1.0 O A:HOH2219 4.5 8.9 1.0 O B:HOH2116 4.5 9.9 1.0 CG B:GLU198 4.5 17.6 1.0 O A:HOH2209 4.6 27.0 1.0 CG B:ASP173 4.7 15.9 1.0 CB B:GLU198 4.8 15.9 1.0 O B:HOH2480 4.9 36.8 1.0 CA A:ASP369 5.0 15.7 1.0

Magnesium binding site 2 out of 2 in the Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength


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 Fully Oxidized State Measured at 1.7470 Angstrom Wavelength within 5.0Å range: probe atom residue distance (Å) B Occ N:Mg518 b:18.4 occ:1.00 NE2 N:HIS368 2.0 22.4 1.0 OD1 N:ASP369 2.1 19.3 1.0 OE1 O:GLU198 2.1 23.8 1.0 O O:HOH3266 2.3 20.7 1.0 O O:HOH3268 2.4 18.4 1.0 O O:HOH3267 2.4 18.3 1.0 CD2 N:HIS368 2.9 20.4 1.0 CE1 N:HIS368 3.0 17.9 1.0 CG N:ASP369 3.3 20.1 1.0 CD O:GLU198 3.3 24.1 1.0 OE2 O:GLU198 3.8 23.6 1.0 O O:SER197 3.9 20.1 1.0 CB N:ASP369 3.9 18.5 1.0 O N:HOH3278 4.0 15.3 1.0 CG N:HIS368 4.0 18.5 1.0 ND1 N:HIS368 4.0 17.2 1.0 OD2 O:ASP173 4.3 24.6 1.0 O N:HOH3297 4.3 9.3 1.0 OD2 N:ASP369 4.3 22.0 1.0 O N:HOH3116 4.3 12.3 1.0 OG1 N:THR294 4.4 19.9 1.0 O N:HOH3219 4.4 10.1 1.0 CG O:GLU198 4.5 20.2 1.0 OD1 O:ASP173 4.5 24.0 1.0 O N:HOH3209 4.6 17.9 1.0 CB O:GLU198 4.7 19.7 1.0 CG O:ASP173 4.8 21.1 1.0 CA N:ASP369 4.9 19.2 1.0

M.Suga, N.Yano, K.Muramoto, K.Shinzawa-Itoh, T.Maeda, E.Yamashita, T.Tsukihara, S.Yoshikawa. Distinguishing Between Cl- and O2(2-) As the Bridging Element Between FE3+ and CU2+ in Resting-Oxidized Cytochrome C Oxidase Acta Crystallogr.,Sect.D V. 67 742 2011.
ISSN: ISSN 0907-4449
PubMed: 21795816
DOI: 10.1107/S0907444911022803