Iron in PDB 2dge: Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana
Protein crystallography data
The structure of Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana, PDB code: 2dge
was solved by
H.Chida,
T.Yokoyama,
F.Kawai,
A.Nakazawa,
H.Akazaki,
Y.Takayama,
T.Hirano,
K.Suruga,
T.Satoh,
S.Yamada,
R.Kawachi,
S.Unzai,
T.Nishio,
S.-Y.Park,
T.Oku,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
31.47 /
1.50
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
50.443,
51.843,
53.685,
82.51,
62.08,
63.26
|
R / Rfree (%)
|
18.6 /
21.5
|
Other elements in 2dge:
The structure of Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana
(pdb code 2dge). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana, PDB code: 2dge:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 2dge
Go back to
Iron Binding Sites List in 2dge
Iron binding site 1 out
of 4 in the Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe200
b:14.4
occ:1.00
|
FE
|
A:HEM200
|
0.0
|
14.4
|
1.0
|
NE2
|
A:HIS90
|
2.0
|
14.2
|
1.0
|
NC
|
A:HEM200
|
2.0
|
14.2
|
1.0
|
NA
|
A:HEM200
|
2.0
|
15.0
|
1.0
|
NB
|
A:HEM200
|
2.0
|
12.8
|
1.0
|
ND
|
A:HEM200
|
2.0
|
14.2
|
1.0
|
SD
|
A:MET130
|
2.3
|
15.9
|
1.0
|
CD2
|
A:HIS90
|
2.9
|
13.6
|
1.0
|
CE1
|
A:HIS90
|
3.0
|
14.7
|
1.0
|
C1A
|
A:HEM200
|
3.0
|
13.9
|
1.0
|
C4C
|
A:HEM200
|
3.0
|
13.9
|
1.0
|
C4A
|
A:HEM200
|
3.0
|
13.6
|
1.0
|
C1C
|
A:HEM200
|
3.0
|
14.1
|
1.0
|
C1B
|
A:HEM200
|
3.0
|
12.8
|
1.0
|
C1D
|
A:HEM200
|
3.0
|
16.4
|
1.0
|
C4D
|
A:HEM200
|
3.1
|
14.9
|
1.0
|
C4B
|
A:HEM200
|
3.1
|
12.7
|
1.0
|
CG
|
A:MET130
|
3.4
|
15.1
|
1.0
|
CHB
|
A:HEM200
|
3.4
|
13.0
|
1.0
|
CHD
|
A:HEM200
|
3.4
|
15.3
|
1.0
|
CHA
|
A:HEM200
|
3.4
|
15.9
|
1.0
|
CHC
|
A:HEM200
|
3.4
|
13.7
|
1.0
|
CE
|
A:MET130
|
3.5
|
15.0
|
1.0
|
ND1
|
A:HIS90
|
4.1
|
13.8
|
1.0
|
CG
|
A:HIS90
|
4.1
|
15.1
|
1.0
|
CB
|
A:MET130
|
4.1
|
14.8
|
1.0
|
C2C
|
A:HEM200
|
4.2
|
16.0
|
1.0
|
C2A
|
A:HEM200
|
4.2
|
14.0
|
1.0
|
C3A
|
A:HEM200
|
4.2
|
13.9
|
1.0
|
C3C
|
A:HEM200
|
4.3
|
15.8
|
1.0
|
C2B
|
A:HEM200
|
4.3
|
13.7
|
1.0
|
C2D
|
A:HEM200
|
4.3
|
15.3
|
1.0
|
C3B
|
A:HEM200
|
4.3
|
13.6
|
1.0
|
C3D
|
A:HEM200
|
4.3
|
17.1
|
1.0
|
|
Iron binding site 2 out
of 4 in 2dge
Go back to
Iron Binding Sites List in 2dge
Iron binding site 2 out
of 4 in the Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe200
b:13.0
occ:1.00
|
FE
|
B:HEM200
|
0.0
|
13.0
|
1.0
|
NE2
|
B:HIS90
|
1.9
|
11.3
|
1.0
|
NB
|
B:HEM200
|
2.0
|
11.1
|
1.0
|
NA
|
B:HEM200
|
2.0
|
13.7
|
1.0
|
ND
|
B:HEM200
|
2.1
|
12.5
|
1.0
|
NC
|
B:HEM200
|
2.1
|
13.4
|
1.0
|
SD
|
B:MET130
|
2.3
|
12.7
|
1.0
|
CE1
|
B:HIS90
|
2.9
|
13.3
|
1.0
|
CD2
|
B:HIS90
|
2.9
|
11.6
|
1.0
|
C4D
|
B:HEM200
|
3.0
|
12.6
|
1.0
|
C1B
|
B:HEM200
|
3.0
|
12.0
|
1.0
|
C1A
|
B:HEM200
|
3.1
|
11.7
|
1.0
|
C4B
|
B:HEM200
|
3.1
|
12.3
|
1.0
|
C1C
|
B:HEM200
|
3.1
|
13.8
|
1.0
|
C1D
|
B:HEM200
|
3.1
|
13.6
|
1.0
|
C4A
|
B:HEM200
|
3.1
|
13.1
|
1.0
|
C4C
|
B:HEM200
|
3.1
|
13.2
|
1.0
|
CHA
|
B:HEM200
|
3.4
|
13.4
|
1.0
|
CG
|
B:MET130
|
3.4
|
14.6
|
1.0
|
CHB
|
B:HEM200
|
3.4
|
11.1
|
1.0
|
CHC
|
B:HEM200
|
3.4
|
13.8
|
1.0
|
CE
|
B:MET130
|
3.4
|
13.8
|
1.0
|
CHD
|
B:HEM200
|
3.5
|
14.4
|
1.0
|
ND1
|
B:HIS90
|
4.0
|
12.4
|
1.0
|
CG
|
B:HIS90
|
4.1
|
12.6
|
1.0
|
CB
|
B:MET130
|
4.2
|
15.3
|
1.0
|
C3D
|
B:HEM200
|
4.3
|
14.1
|
1.0
|
C2B
|
B:HEM200
|
4.3
|
10.5
|
1.0
|
C2D
|
B:HEM200
|
4.3
|
14.1
|
1.0
|
C3B
|
B:HEM200
|
4.3
|
11.5
|
1.0
|
C2A
|
B:HEM200
|
4.3
|
13.4
|
1.0
|
C3A
|
B:HEM200
|
4.3
|
13.1
|
1.0
|
C2C
|
B:HEM200
|
4.3
|
16.1
|
1.0
|
C3C
|
B:HEM200
|
4.3
|
15.6
|
1.0
|
|
Iron binding site 3 out
of 4 in 2dge
Go back to
Iron Binding Sites List in 2dge
Iron binding site 3 out
of 4 in the Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe200
b:10.3
occ:1.00
|
FE
|
C:HEM200
|
0.0
|
10.3
|
1.0
|
NE2
|
C:HIS90
|
1.9
|
10.0
|
1.0
|
ND
|
C:HEM200
|
2.0
|
10.8
|
1.0
|
NB
|
C:HEM200
|
2.0
|
9.8
|
1.0
|
NA
|
C:HEM200
|
2.0
|
11.3
|
1.0
|
NC
|
C:HEM200
|
2.0
|
10.6
|
1.0
|
SD
|
C:MET130
|
2.3
|
14.3
|
1.0
|
CD2
|
C:HIS90
|
2.9
|
11.8
|
1.0
|
CE1
|
C:HIS90
|
3.0
|
9.5
|
1.0
|
C4D
|
C:HEM200
|
3.0
|
10.4
|
1.0
|
C1A
|
C:HEM200
|
3.0
|
10.1
|
1.0
|
C1D
|
C:HEM200
|
3.0
|
11.9
|
1.0
|
C1B
|
C:HEM200
|
3.1
|
9.0
|
1.0
|
C1C
|
C:HEM200
|
3.1
|
11.1
|
1.0
|
C4B
|
C:HEM200
|
3.1
|
9.8
|
1.0
|
C4C
|
C:HEM200
|
3.1
|
11.3
|
1.0
|
C4A
|
C:HEM200
|
3.1
|
9.9
|
1.0
|
CG
|
C:MET130
|
3.4
|
14.8
|
1.0
|
CHA
|
C:HEM200
|
3.4
|
10.4
|
1.0
|
CE
|
C:MET130
|
3.4
|
11.3
|
1.0
|
CHD
|
C:HEM200
|
3.4
|
11.3
|
1.0
|
CHB
|
C:HEM200
|
3.4
|
9.4
|
1.0
|
CHC
|
C:HEM200
|
3.4
|
11.8
|
1.0
|
CB
|
C:MET130
|
4.1
|
16.2
|
1.0
|
ND1
|
C:HIS90
|
4.1
|
10.1
|
1.0
|
CG
|
C:HIS90
|
4.1
|
10.4
|
1.0
|
C3D
|
C:HEM200
|
4.3
|
12.4
|
1.0
|
C2D
|
C:HEM200
|
4.3
|
12.4
|
1.0
|
C2B
|
C:HEM200
|
4.3
|
8.3
|
1.0
|
C2C
|
C:HEM200
|
4.3
|
13.3
|
1.0
|
C2A
|
C:HEM200
|
4.3
|
11.0
|
1.0
|
C3A
|
C:HEM200
|
4.3
|
11.5
|
1.0
|
C3C
|
C:HEM200
|
4.3
|
12.7
|
1.0
|
C3B
|
C:HEM200
|
4.3
|
10.7
|
1.0
|
|
Iron binding site 4 out
of 4 in 2dge
Go back to
Iron Binding Sites List in 2dge
Iron binding site 4 out
of 4 in the Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure of Oxidized Cytochrome C6A From Arabidopsis Thaliana within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe200
b:11.4
occ:1.00
|
FE
|
D:HEM200
|
0.0
|
11.4
|
1.0
|
NE2
|
D:HIS90
|
1.9
|
11.5
|
1.0
|
NA
|
D:HEM200
|
2.0
|
10.7
|
1.0
|
ND
|
D:HEM200
|
2.0
|
10.9
|
1.0
|
NC
|
D:HEM200
|
2.0
|
11.1
|
1.0
|
NB
|
D:HEM200
|
2.0
|
11.2
|
1.0
|
SD
|
D:MET130
|
2.3
|
15.0
|
1.0
|
CE1
|
D:HIS90
|
2.9
|
10.5
|
1.0
|
CD2
|
D:HIS90
|
2.9
|
11.7
|
1.0
|
C1D
|
D:HEM200
|
3.0
|
11.5
|
1.0
|
C1A
|
D:HEM200
|
3.1
|
11.2
|
1.0
|
C4D
|
D:HEM200
|
3.1
|
11.6
|
1.0
|
C1C
|
D:HEM200
|
3.1
|
10.5
|
1.0
|
C1B
|
D:HEM200
|
3.1
|
10.8
|
1.0
|
C4B
|
D:HEM200
|
3.1
|
10.3
|
1.0
|
C4C
|
D:HEM200
|
3.1
|
10.8
|
1.0
|
C4A
|
D:HEM200
|
3.1
|
10.8
|
1.0
|
CE
|
D:MET130
|
3.4
|
14.4
|
1.0
|
CHD
|
D:HEM200
|
3.4
|
12.2
|
1.0
|
CHA
|
D:HEM200
|
3.4
|
11.1
|
1.0
|
CHC
|
D:HEM200
|
3.4
|
9.3
|
1.0
|
CHB
|
D:HEM200
|
3.4
|
11.0
|
1.0
|
CG
|
D:MET130
|
3.5
|
17.4
|
1.0
|
ND1
|
D:HIS90
|
4.0
|
13.4
|
1.0
|
CG
|
D:HIS90
|
4.1
|
11.8
|
1.0
|
CB
|
D:MET130
|
4.1
|
18.2
|
1.0
|
C2D
|
D:HEM200
|
4.3
|
13.4
|
1.0
|
C2A
|
D:HEM200
|
4.3
|
12.0
|
1.0
|
C2B
|
D:HEM200
|
4.3
|
11.3
|
1.0
|
C2C
|
D:HEM200
|
4.3
|
11.9
|
1.0
|
C3D
|
D:HEM200
|
4.3
|
13.3
|
1.0
|
C3A
|
D:HEM200
|
4.3
|
10.9
|
1.0
|
C3B
|
D:HEM200
|
4.3
|
11.1
|
1.0
|
C3C
|
D:HEM200
|
4.3
|
13.2
|
1.0
|
CA
|
D:MET130
|
4.7
|
18.5
|
1.0
|
|
Reference:
H.Chida,
T.Yokoyama,
F.Kawai,
A.Nakazawa,
H.Akazaki,
Y.Takayama,
T.Hirano,
K.Suruga,
T.Satoh,
S.Yamada,
R.Kawachi,
S.Unzai,
T.Nishio,
S.-Y.Park,
T.Oku.
Crystal Structure of Oxidized Cytochrome C(6A) From Arabidopsis Thaliana Febs Lett. V. 580 3763 2006.
ISSN: ISSN 0014-5793
PubMed: 16777100
DOI: 10.1016/J.FEBSLET.2006.05.067
Page generated: Sat Aug 3 20:46:01 2024
|