Iron in PDB 6jy3: Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State

All present enzymatic activity of Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State:
1.9.3.1;

The structure of Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State, PDB code: 6jy3 was solved by K.Shinzawa-Itoh, K.Muramoto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	149.529, 152.131, 174.083, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 19.2

The structure of Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Zinc	(Zn)	1 atom
Copper	(Cu)	3 atoms
Sodium	(Na)	2 atoms

The binding sites of Iron atom in the Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State (pdb code 6jy3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State, PDB code: 6jy3:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:28.3 occ:1.00 FE A:HEA601 0.0 28.3 1.0 NC A:HEA601 2.0 28.0 1.0 NA A:HEA601 2.0 26.3 1.0 NE2 A:HIS61 2.0 29.5 1.0 NB A:HEA601 2.1 28.8 1.0 NE2 A:HIS378 2.1 26.2 1.0 ND A:HEA601 2.1 26.0 1.0 CE1 A:HIS378 3.0 25.9 1.0 C4C A:HEA601 3.0 27.3 1.0 C4A A:HEA601 3.0 30.9 1.0 CE1 A:HIS61 3.0 28.9 1.0 C1C A:HEA601 3.0 26.6 1.0 CD2 A:HIS61 3.0 29.8 1.0 C1B A:HEA601 3.0 33.0 1.0 C1D A:HEA601 3.0 28.2 1.0 C4B A:HEA601 3.1 26.2 1.0 C1A A:HEA601 3.1 27.1 1.0 CD2 A:HIS378 3.1 27.9 1.0 C4D A:HEA601 3.1 26.2 1.0 CHB A:HEA601 3.3 28.6 1.0 CHD A:HEA601 3.4 25.0 1.0 CHC A:HEA601 3.4 26.6 1.0 CHA A:HEA601 3.5 27.7 1.0 ND1 A:HIS61 4.1 30.0 1.0 ND1 A:HIS378 4.1 29.5 1.0 CG A:HIS61 4.2 29.2 1.0 C3A A:HEA601 4.2 28.9 1.0 C3C A:HEA601 4.2 26.6 1.0 C2C A:HEA601 4.2 29.2 1.0 C2A A:HEA601 4.2 29.3 1.0 CG A:HIS378 4.2 27.4 1.0 C3B A:HEA601 4.3 29.1 1.0 C2B A:HEA601 4.3 27.7 1.0 C2D A:HEA601 4.3 24.6 1.0 C3D A:HEA601 4.4 25.4 1.0 CE2 A:PHE377 4.9 29.4 1.0

Iron binding site 2 out of 2 in the Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:26.2 occ:1.00 FE A:HEA602 0.0 26.2 1.0 NA A:HEA602 2.0 25.0 1.0 NC A:HEA602 2.0 25.9 1.0 NB A:HEA602 2.0 23.2 1.0 ND A:HEA602 2.1 25.7 1.0 NE2 A:HIS376 2.1 26.9 1.0 O1 A:PER607 2.2 25.1 1.0 C1B A:HEA602 3.0 26.7 1.0 C1A A:HEA602 3.0 25.6 1.0 C4A A:HEA602 3.0 25.8 1.0 C1C A:HEA602 3.0 28.2 1.0 C1D A:HEA602 3.1 26.8 1.0 C4B A:HEA602 3.1 22.7 1.0 C4D A:HEA602 3.1 25.9 1.0 C4C A:HEA602 3.1 27.9 1.0 CD2 A:HIS376 3.1 29.0 1.0 CE1 A:HIS376 3.1 28.0 1.0 CHB A:HEA602 3.4 24.6 1.0 CHD A:HEA602 3.4 25.3 1.0 CHC A:HEA602 3.4 25.1 1.0 CHA A:HEA602 3.5 22.6 1.0 O2 A:PER607 3.6 33.6 1.0 C2A A:HEA602 4.2 24.7 1.0 ND1 A:HIS376 4.2 25.8 1.0 C2C A:HEA602 4.3 29.3 1.0 CG A:HIS376 4.3 26.7 1.0 C3A A:HEA602 4.3 29.1 1.0 C3C A:HEA602 4.3 27.8 1.0 C3B A:HEA602 4.3 24.5 1.0 C2B A:HEA602 4.3 21.9 1.0 C2D A:HEA602 4.3 23.5 1.0 C3D A:HEA602 4.3 24.6 1.0 CU A:CU603 4.8 26.7 1.0 CG2 A:VAL243 4.9 26.1 1.0

K.Shinzawa-Itoh, T.Sugimura, T.Misaki, Y.Tadehara, S.Yamamoto, M.Hanada, N.Yano, T.Nakagawa, S.Uene, T.Yamada, H.Aoyama, E.Yamashita, T.Tsukihara, S.Yoshikawa, K.Muramoto. Monomeric Structure of An Active Form of Bovine Cytochromecoxidase. Proc.Natl.Acad.Sci.Usa V. 116 19945 2019.
ISSN: ESSN 1091-6490
PubMed: 31533957
DOI: 10.1073/PNAS.1907183116