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Iron in PDB 3ag2: Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
All present enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K:
1.9.3.1;
1.9.3.1;
Protein crystallography data
The structure of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K, PDB code: 3ag2
was solved by
K.Muramoto,
K.Ohta,
K.Shinzawa-Itoh,
K.Kanda,
M.Taniguchi,
H.Nabekura,
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) | 40.00 / 1.80 |
| Space group | P 21 21 21 |
| Cell size a, b, c (Å), α, β, γ (°) | 182.834, 206.933, 178.090, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 19.2 / 22.3 |
Other elements in 3ag2:
The structure of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K also contains other interesting chemical elements:
| Magnesium | (Mg) | 2 atoms |
| Zinc | (Zn) | 2 atoms |
| Copper | (Cu) | 6 atoms |
| Sodium | (Na) | 2 atoms |
Iron Binding Sites:
The binding sites of Iron atom in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
(pdb code 3ag2). 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 the Carbon Monoxide-Bound Fully Reduced State at 100 K, PDB code: 3ag2:
Jump to Iron binding site number: 1; 2; 3; 4;
In total 4 binding sites of Iron where determined in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K, PDB code: 3ag2:
Jump to Iron binding site number: 1; 2; 3; 4;
Iron binding site 1 out of 4 in 3ag2
Go back to
Iron Binding Sites List in 3ag2
Iron binding site 1 out
of 4 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Mono view
Stereo pair view
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 the Carbon Monoxide-Bound Fully Reduced State at 100 K within 5.0Å range:
|
Iron binding site 2 out of 4 in 3ag2
Go back to
Iron Binding Sites List in 3ag2
Iron binding site 2 out
of 4 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Mono view
Stereo pair view
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 the Carbon Monoxide-Bound Fully Reduced State at 100 K within 5.0Å range:
|
Iron binding site 3 out of 4 in 3ag2
Go back to
Iron Binding Sites List in 3ag2
Iron binding site 3 out
of 4 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Mono view
Stereo pair view
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 the Carbon Monoxide-Bound Fully Reduced State at 100 K within 5.0Å range:
|
Iron binding site 4 out of 4 in 3ag2
Go back to
Iron Binding Sites List in 3ag2
Iron binding site 4 out
of 4 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Mono view
Stereo pair view
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 the Carbon Monoxide-Bound Fully Reduced State at 100 K within 5.0Å range:
|
Reference:
K.Muramoto,
K.Ohta,
K.Shinzawa-Itoh,
K.Kanda,
M.Taniguchi,
H.Nabekura,
E.Yamashita,
T.Tsukihara,
S.Yoshikawa.
Bovine Cytochrome C Oxidase Structures Enable O2 Reduction with Minimization of Reactive Oxygens and Provide A Proton-Pumping Gate Proc.Natl.Acad.Sci.Usa V. 107 7740 2010.
ISSN: ISSN 0027-8424
PubMed: 20385840
DOI: 10.1073/PNAS.0910410107
Page generated: Sun Aug 4 07:09:15 2024
ISSN: ISSN 0027-8424
PubMed: 20385840
DOI: 10.1073/PNAS.0910410107
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