Iron in PDB 1oco: Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State

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

The structure of Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State, PDB code: 1oco 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 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	189.100, 210.500, 178.600, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 25.6

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

Magnesium	(Mg)	2 atoms
Zinc	(Zn)	2 atoms
Copper	(Cu)	6 atoms
Sodium	(Na)	2 atoms

The binding sites of Iron atom in the Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State (pdb code 1oco). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State, PDB code: 1oco:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe515 b:13.1 occ:1.00 FE A:HEA515 0.0 13.1 1.0 NE2 A:HIS61 1.9 7.0 1.0 ND A:HEA515 1.9 17.9 1.0 NA A:HEA515 1.9 26.7 1.0 NE2 A:HIS378 1.9 7.0 1.0 NB A:HEA515 1.9 23.4 1.0 NC A:HEA515 2.0 30.1 1.0 CE1 A:HIS378 2.7 16.4 1.0 CD2 A:HIS61 2.8 12.2 1.0 CE1 A:HIS61 2.9 7.0 1.0 C4A A:HEA515 2.9 23.6 1.0 C1B A:HEA515 3.0 27.3 1.0 C1D A:HEA515 3.0 22.2 1.0 C4D A:HEA515 3.0 23.7 1.0 C1A A:HEA515 3.0 21.4 1.0 C4C A:HEA515 3.1 26.4 1.0 C1C A:HEA515 3.1 27.6 1.0 C4B A:HEA515 3.1 24.5 1.0 CD2 A:HIS378 3.1 15.3 1.0 CHB A:HEA515 3.3 26.0 1.0 CHA A:HEA515 3.4 22.1 1.0 CHD A:HEA515 3.4 23.5 1.0 CHC A:HEA515 3.5 28.5 1.0 ND1 A:HIS378 4.0 13.3 1.0 CG A:HIS61 4.1 10.1 1.0 ND1 A:HIS61 4.1 9.6 1.0 C3A A:HEA515 4.2 17.6 1.0 C3D A:HEA515 4.2 22.3 1.0 C2A A:HEA515 4.2 18.6 1.0 C2D A:HEA515 4.2 23.0 1.0 C2B A:HEA515 4.2 32.7 1.0 CG A:HIS378 4.2 7.0 1.0 C3C A:HEA515 4.3 26.4 1.0 C2C A:HEA515 4.3 26.8 1.0 C3B A:HEA515 4.4 28.1 1.0 CE1 A:PHE377 4.8 19.4 1.0

Iron binding site 2 out of 4 in the Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe516 b:7.0 occ:1.00 FE A:HEA516 0.0 7.0 1.0 ND A:HEA516 1.8 7.0 1.0 NB A:HEA516 1.9 7.0 1.0 C A:CMO520 1.9 12.2 1.0 NC A:HEA516 2.0 19.6 1.0 NA A:HEA516 2.0 14.6 1.0 NE2 A:HIS376 2.1 10.8 1.0 C1D A:HEA516 2.9 12.6 1.0 CE1 A:HIS376 2.9 9.1 1.0 C4D A:HEA516 2.9 11.3 1.0 C1B A:HEA516 2.9 10.8 1.0 C4B A:HEA516 3.0 12.4 1.0 C4C A:HEA516 3.0 14.9 1.0 C1C A:HEA516 3.1 16.2 1.0 O A:CMO520 3.1 19.1 1.0 C4A A:HEA516 3.1 7.7 1.0 C1A A:HEA516 3.1 7.0 1.0 CD2 A:HIS376 3.2 7.5 1.0 CHD A:HEA516 3.3 16.6 1.0 CHB A:HEA516 3.4 11.2 1.0 CHA A:HEA516 3.4 7.0 1.0 CHC A:HEA516 3.4 8.8 1.0 C3D A:HEA516 4.1 13.2 1.0 C2D A:HEA516 4.1 13.4 1.0 ND1 A:HIS376 4.1 7.8 1.0 C2B A:HEA516 4.2 7.0 1.0 C3B A:HEA516 4.2 9.8 1.0 CG A:HIS376 4.2 7.2 1.0 C3C A:HEA516 4.3 17.5 1.0 C2C A:HEA516 4.3 14.2 1.0 C3A A:HEA516 4.3 7.0 1.0 C2A A:HEA516 4.4 7.0 1.0

Iron binding site 3 out of 4 in the Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ N:Fe515 b:31.2 occ:1.00 FE N:HEA515 0.0 31.2 1.0 NE2 N:HIS61 1.7 10.3 1.0 NA N:HEA515 1.9 28.6 1.0 NB N:HEA515 1.9 35.1 1.0 ND N:HEA515 1.9 28.6 1.0 NC N:HEA515 2.0 27.1 1.0 NE2 N:HIS378 2.1 22.7 1.0 CD2 N:HIS61 2.7 15.0 1.0 CE1 N:HIS61 2.7 20.9 1.0 CE1 N:HIS378 2.9 13.9 1.0 C4A N:HEA515 2.9 27.1 1.0 C1B N:HEA515 2.9 35.6 1.0 C1A N:HEA515 3.0 32.9 1.0 C4D N:HEA515 3.0 30.1 1.0 C1D N:HEA515 3.0 28.6 1.0 C4C N:HEA515 3.0 32.1 1.0 C1C N:HEA515 3.0 32.8 1.0 C4B N:HEA515 3.1 35.0 1.0 CHB N:HEA515 3.3 30.5 1.0 CD2 N:HIS378 3.3 21.8 1.0 CHA N:HEA515 3.4 33.1 1.0 CHD N:HEA515 3.4 29.8 1.0 CHC N:HEA515 3.4 34.8 1.0 CG N:HIS61 3.9 19.6 1.0 ND1 N:HIS61 4.0 18.9 1.0 C3A N:HEA515 4.2 26.5 1.0 C2B N:HEA515 4.2 34.3 1.0 C2A N:HEA515 4.2 23.9 1.0 C3D N:HEA515 4.2 30.2 1.0 ND1 N:HIS378 4.2 11.4 1.0 C2D N:HEA515 4.2 27.0 1.0 C2C N:HEA515 4.3 37.6 1.0 C3C N:HEA515 4.3 36.3 1.0 C3B N:HEA515 4.3 33.0 1.0 CG N:HIS378 4.4 19.2 1.0

Iron binding site 4 out of 4 in the Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Bovine Heart Cytochrome C Oxidase in Carbon Monoxide-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ N:Fe516 b:7.4 occ:1.00 FE N:HEA516 0.0 7.4 1.0 NB N:HEA516 1.8 7.0 1.0 ND N:HEA516 1.9 7.0 1.0 C N:CMO520 1.9 11.7 1.0 NA N:HEA516 2.0 12.5 1.0 NC N:HEA516 2.0 14.3 1.0 NE2 N:HIS376 2.1 23.9 1.0 O N:CMO520 2.9 22.4 1.0 C1B N:HEA516 2.9 13.4 1.0 CE1 N:HIS376 2.9 22.0 1.0 C1D N:HEA516 2.9 17.5 1.0 C4B N:HEA516 2.9 8.0 1.0 C4D N:HEA516 3.0 10.4 1.0 C4A N:HEA516 3.0 14.1 1.0 C1C N:HEA516 3.1 15.6 1.0 C4C N:HEA516 3.1 18.7 1.0 C1A N:HEA516 3.1 8.3 1.0 CD2 N:HIS376 3.2 22.8 1.0 CHB N:HEA516 3.3 15.1 1.0 CHC N:HEA516 3.4 7.0 1.0 CHD N:HEA516 3.4 19.2 1.0 CHA N:HEA516 3.4 9.7 1.0 ND1 N:HIS376 4.1 22.7 1.0 C2B N:HEA516 4.1 10.7 1.0 C3D N:HEA516 4.2 10.9 1.0 C3B N:HEA516 4.2 16.3 1.0 C3A N:HEA516 4.2 13.9 1.0 C2D N:HEA516 4.2 13.5 1.0 CG N:HIS376 4.3 20.7 1.0 C2A N:HEA516 4.3 14.2 1.0 C2C N:HEA516 4.3 16.2 1.0 C3C N:HEA516 4.3 17.9 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