Iron in PDB 2dyr: Bovine Heart Cytochrome C Oxidase at the Fully Oxidized State
Enzymatic activity of Bovine Heart Cytochrome C Oxidase at the Fully Oxidized State
All present enzymatic activity of Bovine Heart Cytochrome C Oxidase at the Fully Oxidized State:
1.9.3.1;
Protein crystallography data
The structure of Bovine Heart Cytochrome C Oxidase at the Fully Oxidized State, PDB code: 2dyr
was solved by
K.Shinzawa-Itoh,
H.Aoyama,
K.Muramoto,
T.Kurauchi,
T.Mizushima,
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 (°)
|
182.590,
205.140,
178.250,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.2 /
22.7
|
Other elements in 2dyr:
The structure of Bovine Heart Cytochrome C Oxidase at the Fully Oxidized State also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Bovine Heart Cytochrome C Oxidase at the Fully Oxidized State
(pdb code 2dyr). 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 at the Fully Oxidized State, PDB code: 2dyr:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 2dyr
Go back to
Iron Binding Sites List in 2dyr
Iron binding site 1 out
of 4 in the Bovine Heart Cytochrome C Oxidase at 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 Bovine Heart Cytochrome C Oxidase at the Fully Oxidized State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe515
b:20.9
occ:1.00
|
FE
|
A:HEA515
|
0.0
|
20.9
|
1.0
|
NE2
|
A:HIS378
|
1.9
|
13.4
|
1.0
|
NB
|
A:HEA515
|
2.0
|
19.1
|
1.0
|
NE2
|
A:HIS61
|
2.0
|
13.4
|
1.0
|
NC
|
A:HEA515
|
2.0
|
19.5
|
1.0
|
ND
|
A:HEA515
|
2.0
|
20.4
|
1.0
|
NA
|
A:HEA515
|
2.1
|
19.2
|
1.0
|
CE1
|
A:HIS378
|
2.8
|
17.9
|
1.0
|
CE1
|
A:HIS61
|
3.0
|
15.9
|
1.0
|
C1B
|
A:HEA515
|
3.0
|
21.8
|
1.0
|
C4B
|
A:HEA515
|
3.0
|
20.8
|
1.0
|
CD2
|
A:HIS61
|
3.0
|
19.1
|
1.0
|
C4C
|
A:HEA515
|
3.0
|
20.4
|
1.0
|
C1C
|
A:HEA515
|
3.1
|
20.7
|
1.0
|
CD2
|
A:HIS378
|
3.1
|
17.8
|
1.0
|
C4A
|
A:HEA515
|
3.1
|
20.2
|
1.0
|
C1D
|
A:HEA515
|
3.1
|
22.8
|
1.0
|
C4D
|
A:HEA515
|
3.1
|
23.4
|
1.0
|
C1A
|
A:HEA515
|
3.1
|
21.3
|
1.0
|
CHC
|
A:HEA515
|
3.4
|
21.4
|
1.0
|
CHB
|
A:HEA515
|
3.4
|
19.6
|
1.0
|
CHD
|
A:HEA515
|
3.4
|
19.0
|
1.0
|
CHA
|
A:HEA515
|
3.5
|
23.3
|
1.0
|
ND1
|
A:HIS378
|
4.0
|
17.6
|
1.0
|
ND1
|
A:HIS61
|
4.1
|
16.4
|
1.0
|
CG
|
A:HIS378
|
4.1
|
16.2
|
1.0
|
CG
|
A:HIS61
|
4.2
|
16.5
|
1.0
|
C2B
|
A:HEA515
|
4.2
|
20.1
|
1.0
|
C3B
|
A:HEA515
|
4.3
|
19.2
|
1.0
|
C3C
|
A:HEA515
|
4.3
|
20.2
|
1.0
|
C2C
|
A:HEA515
|
4.3
|
19.6
|
1.0
|
C3A
|
A:HEA515
|
4.3
|
21.1
|
1.0
|
C2A
|
A:HEA515
|
4.3
|
20.2
|
1.0
|
C3D
|
A:HEA515
|
4.3
|
22.3
|
1.0
|
C2D
|
A:HEA515
|
4.3
|
19.9
|
1.0
|
CE2
|
A:PHE377
|
5.0
|
19.9
|
1.0
|
|
Iron binding site 2 out
of 4 in 2dyr
Go back to
Iron Binding Sites List in 2dyr
Iron binding site 2 out
of 4 in the Bovine Heart Cytochrome C Oxidase at 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 Bovine Heart Cytochrome C Oxidase at the Fully Oxidized State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe516
b:17.8
occ:1.00
|
FE
|
A:HEA516
|
0.0
|
17.8
|
1.0
|
ND
|
A:HEA516
|
1.9
|
19.2
|
1.0
|
NB
|
A:HEA516
|
1.9
|
18.3
|
1.0
|
NA
|
A:HEA516
|
2.0
|
19.0
|
1.0
|
NC
|
A:HEA516
|
2.1
|
18.8
|
1.0
|
NE2
|
A:HIS376
|
2.1
|
17.8
|
1.0
|
CE1
|
A:HIS376
|
3.0
|
20.8
|
1.0
|
C4D
|
A:HEA516
|
3.0
|
20.2
|
1.0
|
C1B
|
A:HEA516
|
3.0
|
19.4
|
1.0
|
C4B
|
A:HEA516
|
3.0
|
21.9
|
1.0
|
C1D
|
A:HEA516
|
3.0
|
20.3
|
1.0
|
C4A
|
A:HEA516
|
3.1
|
17.9
|
1.0
|
C1A
|
A:HEA516
|
3.1
|
16.5
|
1.0
|
C1C
|
A:HEA516
|
3.1
|
20.6
|
1.0
|
C4C
|
A:HEA516
|
3.1
|
17.4
|
1.0
|
CD2
|
A:HIS376
|
3.2
|
18.5
|
1.0
|
CHB
|
A:HEA516
|
3.4
|
21.3
|
1.0
|
CHA
|
A:HEA516
|
3.4
|
17.2
|
1.0
|
CHC
|
A:HEA516
|
3.4
|
21.6
|
1.0
|
CHD
|
A:HEA516
|
3.5
|
17.2
|
1.0
|
ND1
|
A:HIS376
|
4.2
|
19.8
|
1.0
|
C2B
|
A:HEA516
|
4.2
|
18.7
|
1.0
|
C3D
|
A:HEA516
|
4.2
|
18.8
|
1.0
|
C3B
|
A:HEA516
|
4.3
|
21.1
|
1.0
|
C2D
|
A:HEA516
|
4.3
|
18.9
|
1.0
|
CG
|
A:HIS376
|
4.3
|
19.4
|
1.0
|
C2A
|
A:HEA516
|
4.3
|
17.6
|
1.0
|
C3A
|
A:HEA516
|
4.3
|
17.8
|
1.0
|
C3C
|
A:HEA516
|
4.4
|
17.8
|
1.0
|
C2C
|
A:HEA516
|
4.4
|
21.3
|
1.0
|
CU
|
A:CU517
|
5.0
|
20.0
|
1.0
|
|
Iron binding site 3 out
of 4 in 2dyr
Go back to
Iron Binding Sites List in 2dyr
Iron binding site 3 out
of 4 in the Bovine Heart Cytochrome C Oxidase at the Fully Oxidized 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 at the Fully Oxidized State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
N:Fe515
b:20.5
occ:1.00
|
FE
|
N:HEA515
|
0.0
|
20.5
|
1.0
|
NE2
|
N:HIS61
|
1.9
|
16.2
|
1.0
|
NE2
|
N:HIS378
|
2.0
|
17.3
|
1.0
|
NB
|
N:HEA515
|
2.0
|
23.3
|
1.0
|
NC
|
N:HEA515
|
2.0
|
22.8
|
1.0
|
ND
|
N:HEA515
|
2.0
|
22.8
|
1.0
|
NA
|
N:HEA515
|
2.0
|
23.6
|
1.0
|
CE1
|
N:HIS378
|
2.9
|
18.3
|
1.0
|
CE1
|
N:HIS61
|
2.9
|
22.0
|
1.0
|
CD2
|
N:HIS61
|
2.9
|
21.8
|
1.0
|
C1B
|
N:HEA515
|
3.0
|
23.6
|
1.0
|
C4C
|
N:HEA515
|
3.0
|
25.2
|
1.0
|
C4D
|
N:HEA515
|
3.0
|
24.7
|
1.0
|
C4B
|
N:HEA515
|
3.1
|
24.1
|
1.0
|
C1A
|
N:HEA515
|
3.1
|
25.1
|
1.0
|
C4A
|
N:HEA515
|
3.1
|
24.9
|
1.0
|
C1D
|
N:HEA515
|
3.1
|
24.7
|
1.0
|
C1C
|
N:HEA515
|
3.1
|
24.1
|
1.0
|
CD2
|
N:HIS378
|
3.1
|
17.9
|
1.0
|
CHB
|
N:HEA515
|
3.4
|
22.1
|
1.0
|
CHA
|
N:HEA515
|
3.4
|
25.1
|
1.0
|
CHD
|
N:HEA515
|
3.4
|
22.0
|
1.0
|
CHC
|
N:HEA515
|
3.4
|
22.9
|
1.0
|
ND1
|
N:HIS61
|
4.1
|
17.7
|
1.0
|
ND1
|
N:HIS378
|
4.1
|
17.4
|
1.0
|
CG
|
N:HIS61
|
4.1
|
21.6
|
1.0
|
CG
|
N:HIS378
|
4.2
|
16.8
|
1.0
|
C2B
|
N:HEA515
|
4.3
|
24.0
|
1.0
|
C2A
|
N:HEA515
|
4.3
|
23.4
|
1.0
|
C3B
|
N:HEA515
|
4.3
|
24.2
|
1.0
|
C3A
|
N:HEA515
|
4.3
|
24.4
|
1.0
|
C3C
|
N:HEA515
|
4.3
|
24.0
|
1.0
|
C3D
|
N:HEA515
|
4.3
|
22.4
|
1.0
|
C2D
|
N:HEA515
|
4.3
|
23.2
|
1.0
|
C2C
|
N:HEA515
|
4.3
|
24.9
|
1.0
|
CE2
|
N:PHE377
|
4.8
|
21.8
|
1.0
|
|
Iron binding site 4 out
of 4 in 2dyr
Go back to
Iron Binding Sites List in 2dyr
Iron binding site 4 out
of 4 in the Bovine Heart Cytochrome C Oxidase at the Fully Oxidized 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 at the Fully Oxidized State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
N:Fe516
b:20.6
occ:1.00
|
FE
|
N:HEA516
|
0.0
|
20.6
|
1.0
|
ND
|
N:HEA516
|
1.9
|
18.9
|
1.0
|
NB
|
N:HEA516
|
2.0
|
19.2
|
1.0
|
NC
|
N:HEA516
|
2.0
|
22.2
|
1.0
|
NA
|
N:HEA516
|
2.1
|
20.3
|
1.0
|
NE2
|
N:HIS376
|
2.2
|
22.2
|
1.0
|
C4D
|
N:HEA516
|
3.0
|
19.4
|
1.0
|
C1D
|
N:HEA516
|
3.0
|
22.6
|
1.0
|
C4B
|
N:HEA516
|
3.0
|
21.7
|
1.0
|
C1B
|
N:HEA516
|
3.1
|
21.0
|
1.0
|
C4C
|
N:HEA516
|
3.1
|
22.8
|
1.0
|
C1C
|
N:HEA516
|
3.1
|
20.8
|
1.0
|
C1A
|
N:HEA516
|
3.1
|
19.1
|
1.0
|
CD2
|
N:HIS376
|
3.1
|
21.0
|
1.0
|
C4A
|
N:HEA516
|
3.1
|
19.5
|
1.0
|
CE1
|
N:HIS376
|
3.2
|
24.0
|
1.0
|
CHD
|
N:HEA516
|
3.4
|
23.6
|
1.0
|
CHA
|
N:HEA516
|
3.4
|
17.8
|
1.0
|
CHC
|
N:HEA516
|
3.4
|
21.9
|
1.0
|
CHB
|
N:HEA516
|
3.5
|
19.8
|
1.0
|
C3D
|
N:HEA516
|
4.2
|
18.4
|
1.0
|
C2D
|
N:HEA516
|
4.2
|
19.7
|
1.0
|
C2B
|
N:HEA516
|
4.3
|
17.6
|
1.0
|
C3B
|
N:HEA516
|
4.3
|
19.2
|
1.0
|
CG
|
N:HIS376
|
4.3
|
21.6
|
1.0
|
ND1
|
N:HIS376
|
4.3
|
21.2
|
1.0
|
C2C
|
N:HEA516
|
4.3
|
22.6
|
1.0
|
C2A
|
N:HEA516
|
4.4
|
18.8
|
1.0
|
C3C
|
N:HEA516
|
4.4
|
22.7
|
1.0
|
C3A
|
N:HEA516
|
4.4
|
18.8
|
1.0
|
CU
|
N:CU517
|
5.0
|
21.4
|
1.0
|
|
Reference:
K.Shinzawa-Itoh,
H.Aoyama,
K.Muramoto,
H.Terada,
T.Kurauchi,
Y.Tadehara,
A.Yamasaki,
T.Sugimura,
S.Kurono,
K.Tsujimoto,
T.Mizushima,
E.Yamashita,
T.Tsukihara,
S.Yoshikawa.
Structures and Physiological Roles of 13 Integral Lipids of Bovine Heart Cytochrome C Oxidase Embo J. V. 26 1713 2007.
ISSN: ISSN 0261-4189
PubMed: 17332748
DOI: 10.1038/SJ.EMBOJ.7601618
Page generated: Sat Aug 3 20:52:55 2024
|