Iron in PDB 6jy4: Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State

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

The structure of Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State, PDB code: 6jy4 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 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	149.395, 152.395, 174.040, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 20.5

The structure of Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Reduced 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 Reduced State (pdb code 6jy4). 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 Reduced State, PDB code: 6jy4:
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 Reduced 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 Reduced State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:31.9 occ:1.00 FE A:HEA601 0.0 31.9 1.0 NA A:HEA601 2.0 28.7 1.0 NE2 A:HIS61 2.0 33.2 1.0 NC A:HEA601 2.0 30.9 1.0 NB A:HEA601 2.1 31.9 1.0 NE2 A:HIS378 2.1 30.1 1.0 ND A:HEA601 2.1 28.2 1.0 CE1 A:HIS61 3.0 29.2 1.0 CD2 A:HIS61 3.0 33.6 1.0 C4A A:HEA601 3.0 33.6 1.0 C4C A:HEA601 3.0 31.7 1.0 C1B A:HEA601 3.0 36.9 1.0 CE1 A:HIS378 3.0 30.0 1.0 C1C A:HEA601 3.0 29.9 1.0 C1D A:HEA601 3.0 32.2 1.0 C4B A:HEA601 3.0 28.8 1.0 C1A A:HEA601 3.1 26.6 1.0 CD2 A:HIS378 3.1 36.2 1.0 C4D A:HEA601 3.1 33.8 1.0 CHB A:HEA601 3.3 34.7 1.0 CHD A:HEA601 3.3 30.9 1.0 CHC A:HEA601 3.5 32.8 1.0 CHA A:HEA601 3.5 28.2 1.0 ND1 A:HIS61 4.1 34.1 1.0 CG A:HIS61 4.1 30.2 1.0 ND1 A:HIS378 4.2 35.0 1.0 C2A A:HEA601 4.2 33.0 1.0 C3A A:HEA601 4.2 32.4 1.0 C2C A:HEA601 4.2 26.9 1.0 C3C A:HEA601 4.2 33.2 1.0 CG A:HIS378 4.2 31.5 1.0 C3B A:HEA601 4.3 35.0 1.0 C2B A:HEA601 4.3 32.5 1.0 C2D A:HEA601 4.3 33.4 1.0 C3D A:HEA601 4.4 27.7 1.0 OG A:SER382 4.5 48.6 1.0

Iron binding site 2 out of 2 in the Monomeric Form of Bovine Heart Cytochrome C Oxidase in the Fully Reduced 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 Reduced State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:29.3 occ:1.00 FE A:HEA602 0.0 29.3 1.0 NA A:HEA602 2.0 26.7 1.0 NC A:HEA602 2.0 32.2 1.0 NB A:HEA602 2.0 27.3 1.0 ND A:HEA602 2.1 30.8 1.0 NE2 A:HIS376 2.2 31.3 1.0 C1C A:HEA602 3.0 30.3 1.0 C4B A:HEA602 3.0 27.6 1.0 C1B A:HEA602 3.0 29.1 1.0 C1A A:HEA602 3.0 30.9 1.0 C4C A:HEA602 3.0 28.4 1.0 C4A A:HEA602 3.0 32.9 1.0 C1D A:HEA602 3.1 28.4 1.0 C4D A:HEA602 3.1 30.0 1.0 CE1 A:HIS376 3.1 30.5 1.0 CD2 A:HIS376 3.2 32.5 1.0 CHC A:HEA602 3.4 25.7 1.0 CHB A:HEA602 3.4 28.6 1.0 CHD A:HEA602 3.4 30.1 1.0 CHA A:HEA602 3.5 26.7 1.0 C2C A:HEA602 4.2 31.6 1.0 C2A A:HEA602 4.2 27.1 1.0 C2B A:HEA602 4.2 27.9 1.0 C3C A:HEA602 4.3 28.7 1.0 C3A A:HEA602 4.3 31.7 1.0 C3B A:HEA602 4.3 27.9 1.0 ND1 A:HIS376 4.3 30.5 1.0 C3D A:HEA602 4.3 28.8 1.0 CG A:HIS376 4.3 29.9 1.0 C2D A:HEA602 4.3 29.7 1.0 CG1 A:VAL380 4.7 37.6 1.0 CG2 A:VAL243 5.0 30.0 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