Magnesium in PDB 1ocz: Bovine Heart Cytochrome C Oxidase in Azide-Bound State

All present enzymatic activity of Bovine Heart Cytochrome C Oxidase in Azide-Bound State:
1.9.3.1;

The structure of Bovine Heart Cytochrome C Oxidase in Azide-Bound State, PDB code: 1ocz was solved by T.Tsukihara, M.Yao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 2.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	189.200, 210.600, 178.500, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 25.5

The structure of Bovine Heart Cytochrome C Oxidase in Azide-Bound State also contains other interesting chemical elements:

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

The binding sites of Magnesium atom in the Bovine Heart Cytochrome C Oxidase in Azide-Bound State (pdb code 1ocz). 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 Azide-Bound State, PDB code: 1ocz:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Bovine Heart Cytochrome C Oxidase in Azide-Bound State


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 Azide-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg518 b:14.4 occ:1.00 OE1 B:GLU198 2.1 27.3 1.0 OD2 A:ASP369 2.2 24.4 1.0 NE2 A:HIS368 2.3 29.5 1.0 CE1 A:HIS368 2.5 30.8 1.0 CD B:GLU198 3.4 37.6 1.0 CG A:ASP369 3.4 23.4 1.0 CD2 A:HIS368 3.7 36.3 1.0 OD2 B:ASP173 3.7 49.7 1.0 ND1 A:HIS368 3.9 27.4 1.0 OD1 B:ASP173 4.2 35.3 1.0 OE2 B:GLU198 4.2 45.8 1.0 CB A:ASP369 4.3 14.4 1.0 OD1 A:ASP369 4.3 34.1 1.0 CG B:GLU198 4.3 26.7 1.0 CG B:ASP173 4.4 39.8 1.0 O B:SER197 4.4 16.1 1.0 CG A:HIS368 4.4 29.0 1.0 OG1 A:THR294 4.7 27.3 1.0 CB B:GLU198 4.8 19.6 1.0

Magnesium binding site 2 out of 2 in the Bovine Heart Cytochrome C Oxidase in Azide-Bound State


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 Azide-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ N:Mg518 b:30.9 occ:1.00 OE1 O:GLU198 2.1 47.3 1.0 OD2 N:ASP369 2.2 39.1 1.0 NE2 N:HIS368 2.2 45.8 1.0 CE1 N:HIS368 2.6 45.3 1.0 CD O:GLU198 3.4 46.9 1.0 CG N:ASP369 3.4 32.9 1.0 OD2 O:ASP173 3.5 33.4 1.0 CD2 N:HIS368 3.6 50.0 1.0 OD1 O:ASP173 3.9 22.3 1.0 ND1 N:HIS368 4.0 33.8 1.0 O O:SER197 4.1 33.8 1.0 CG O:ASP173 4.1 25.2 1.0 CB N:ASP369 4.2 21.9 1.0 CG O:GLU198 4.2 38.1 1.0 OE2 O:GLU198 4.2 46.6 1.0 OD1 N:ASP369 4.3 39.9 1.0 CG N:HIS368 4.4 38.9 1.0 OG1 N:THR294 4.5 27.0 1.0 CB O:GLU198 4.7 26.6 1.0 CA O:GLU198 5.0 33.7 1.0

S.Yoshikawa, K.Shinzawa-Itoh, R.Nakashima, R.Yaono, E.Yamashita, N.Inoue, M.Yao, M.J.Fei, C.P.Libeu, T.Mizushima, H.Yamaguchi, T.Tomizaki, T.Tsukihara. Redox-Coupled Crystal Structural Changes in Bovine Heart Cytochrome C Oxidase. Science V. 280 1723 1998.
ISSN: ISSN 0036-8075
PubMed: 9624044
DOI: 10.1126/SCIENCE.280.5370.1723