Iron in PDB 2y3q: 1.55A Structure of Apo Bacterioferritin From E. Coli
Protein crystallography data
The structure of 1.55A Structure of Apo Bacterioferritin From E. Coli, PDB code: 2y3q
was solved by
M.A.Hough,
S.V.Antonyuk,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
43.23 /
1.55
|
|
Space group
|
P 42 21 2
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
208.000,
208.000,
142.600,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
16.476 /
20.007
|
Iron Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Iron atom in the 1.55A Structure of Apo Bacterioferritin From E. Coli
(pdb code 2y3q). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 12 binding sites of Iron where determined in the
1.55A Structure of Apo Bacterioferritin From E. Coli, PDB code: 2y3q:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 12 in 2y3q
Go back to
Iron Binding Sites List in 2y3q
Iron binding site 1 out
of 12 in the 1.55A Structure of Apo Bacterioferritin From E. Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of 1.55A Structure of Apo Bacterioferritin From E. Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe200
b:5.4
occ:0.45
|
FE
|
A:HEM200
|
0.0
|
5.4
|
0.5
|
|
FE
|
B:HEM200
|
0.2
|
13.7
|
0.5
|
|
ND
|
B:HEM200
|
1.9
|
13.4
|
0.5
|
|
ND
|
A:HEM200
|
2.0
|
6.3
|
0.5
|
|
NA
|
A:HEM200
|
2.0
|
4.3
|
0.5
|
|
NB
|
A:HEM200
|
2.0
|
4.6
|
0.5
|
|
NA
|
B:HEM200
|
2.0
|
13.1
|
0.5
|
|
NC
|
B:HEM200
|
2.1
|
13.6
|
0.5
|
|
NC
|
A:HEM200
|
2.1
|
5.7
|
0.5
|
|
NB
|
B:HEM200
|
2.3
|
12.2
|
0.5
|
|
SD
|
A:MET52
|
2.3
|
9.2
|
1.0
|
|
SD
|
B:MET52
|
2.3
|
9.2
|
1.0
|
|
C4D
|
B:HEM200
|
2.9
|
13.2
|
0.5
|
|
C1D
|
B:HEM200
|
2.9
|
13.1
|
0.5
|
|
C1A
|
B:HEM200
|
3.0
|
12.3
|
0.5
|
|
C1D
|
A:HEM200
|
3.0
|
5.9
|
0.5
|
|
C4D
|
A:HEM200
|
3.0
|
5.6
|
0.5
|
|
C1B
|
A:HEM200
|
3.0
|
4.7
|
0.5
|
|
C4A
|
A:HEM200
|
3.0
|
3.6
|
0.5
|
|
C1A
|
A:HEM200
|
3.0
|
4.6
|
0.5
|
|
C4C
|
A:HEM200
|
3.1
|
7.0
|
0.5
|
|
C4C
|
B:HEM200
|
3.1
|
14.6
|
0.5
|
|
C4B
|
A:HEM200
|
3.1
|
7.3
|
0.5
|
|
C1C
|
B:HEM200
|
3.1
|
14.4
|
0.5
|
|
C1C
|
A:HEM200
|
3.1
|
7.1
|
0.5
|
|
C4A
|
B:HEM200
|
3.1
|
11.7
|
0.5
|
|
C1B
|
B:HEM200
|
3.3
|
11.4
|
0.5
|
|
C4B
|
B:HEM200
|
3.3
|
12.7
|
0.5
|
|
CHA
|
B:HEM200
|
3.3
|
12.0
|
0.5
|
|
CE
|
B:MET52
|
3.3
|
11.4
|
1.0
|
|
CHD
|
B:HEM200
|
3.4
|
14.4
|
0.5
|
|
CHB
|
A:HEM200
|
3.4
|
5.3
|
0.5
|
|
CHA
|
A:HEM200
|
3.4
|
5.0
|
0.5
|
|
CE
|
A:MET52
|
3.4
|
10.7
|
1.0
|
|
CHD
|
A:HEM200
|
3.4
|
6.7
|
0.5
|
|
CG
|
A:MET52
|
3.4
|
6.0
|
1.0
|
|
CHC
|
A:HEM200
|
3.5
|
7.0
|
0.5
|
|
CHC
|
B:HEM200
|
3.6
|
13.2
|
0.5
|
|
CG
|
B:MET52
|
3.6
|
8.0
|
1.0
|
|
CHB
|
B:HEM200
|
3.6
|
12.5
|
0.5
|
|
C3D
|
B:HEM200
|
4.1
|
14.3
|
0.5
|
|
C2D
|
B:HEM200
|
4.1
|
13.8
|
0.5
|
|
CB
|
A:MET52
|
4.2
|
7.6
|
1.0
|
|
C2D
|
A:HEM200
|
4.2
|
6.7
|
0.5
|
|
C3A
|
A:HEM200
|
4.2
|
4.0
|
0.5
|
|
C2A
|
B:HEM200
|
4.2
|
13.1
|
0.5
|
|
C3D
|
A:HEM200
|
4.2
|
7.7
|
0.5
|
|
C2A
|
A:HEM200
|
4.3
|
5.7
|
0.5
|
|
C2B
|
A:HEM200
|
4.3
|
5.8
|
0.5
|
|
CB
|
B:MET52
|
4.3
|
7.2
|
1.0
|
|
C3B
|
A:HEM200
|
4.3
|
8.0
|
0.5
|
|
C3C
|
A:HEM200
|
4.3
|
10.2
|
0.5
|
|
C3A
|
B:HEM200
|
4.3
|
10.4
|
0.5
|
|
C2C
|
B:HEM200
|
4.3
|
13.9
|
0.5
|
|
C3C
|
B:HEM200
|
4.3
|
15.9
|
0.5
|
|
C2C
|
A:HEM200
|
4.3
|
8.3
|
0.5
|
|
C2B
|
B:HEM200
|
4.5
|
11.9
|
0.5
|
|
C3B
|
B:HEM200
|
4.5
|
13.1
|
0.5
|
|
Iron binding site 2 out
of 12 in 2y3q
Go back to
Iron Binding Sites List in 2y3q
Iron binding site 2 out
of 12 in the 1.55A Structure of Apo Bacterioferritin From E. Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of 1.55A Structure of Apo Bacterioferritin From E. Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe200
b:13.7
occ:0.45
|
FE
|
B:HEM200
|
0.0
|
13.7
|
0.5
|
|
FE
|
A:HEM200
|
0.2
|
5.4
|
0.5
|
|
NC
|
A:HEM200
|
1.9
|
5.7
|
0.5
|
|
ND
|
A:HEM200
|
2.0
|
6.3
|
0.5
|
|
NB
|
A:HEM200
|
2.0
|
4.6
|
0.5
|
|
NA
|
B:HEM200
|
2.0
|
13.1
|
0.5
|
|
NC
|
B:HEM200
|
2.0
|
13.6
|
0.5
|
|
NB
|
B:HEM200
|
2.1
|
12.2
|
0.5
|
|
ND
|
B:HEM200
|
2.1
|
13.4
|
0.5
|
|
NA
|
A:HEM200
|
2.2
|
4.3
|
0.5
|
|
SD
|
B:MET52
|
2.3
|
9.2
|
1.0
|
|
SD
|
A:MET52
|
2.4
|
9.2
|
1.0
|
|
C4C
|
A:HEM200
|
2.9
|
7.0
|
0.5
|
|
C1D
|
A:HEM200
|
2.9
|
5.9
|
0.5
|
|
C1C
|
A:HEM200
|
3.0
|
7.1
|
0.5
|
|
C1C
|
B:HEM200
|
3.0
|
14.4
|
0.5
|
|
C4B
|
A:HEM200
|
3.0
|
7.3
|
0.5
|
|
C1A
|
B:HEM200
|
3.1
|
12.3
|
0.5
|
|
C4D
|
B:HEM200
|
3.1
|
13.2
|
0.5
|
|
C1B
|
A:HEM200
|
3.1
|
4.7
|
0.5
|
|
C4D
|
A:HEM200
|
3.1
|
5.6
|
0.5
|
|
C4B
|
B:HEM200
|
3.1
|
12.7
|
0.5
|
|
C4A
|
B:HEM200
|
3.1
|
11.7
|
0.5
|
|
C1D
|
B:HEM200
|
3.1
|
13.1
|
0.5
|
|
C4C
|
B:HEM200
|
3.1
|
14.6
|
0.5
|
|
C1B
|
B:HEM200
|
3.1
|
11.4
|
0.5
|
|
C4A
|
A:HEM200
|
3.2
|
3.6
|
0.5
|
|
C1A
|
A:HEM200
|
3.2
|
4.6
|
0.5
|
|
CHD
|
A:HEM200
|
3.3
|
6.7
|
0.5
|
|
CE
|
B:MET52
|
3.3
|
11.4
|
1.0
|
|
CE
|
A:MET52
|
3.4
|
10.7
|
1.0
|
|
CHC
|
A:HEM200
|
3.4
|
7.0
|
0.5
|
|
CHA
|
B:HEM200
|
3.4
|
12.0
|
0.5
|
|
CHC
|
B:HEM200
|
3.4
|
13.2
|
0.5
|
|
CG
|
B:MET52
|
3.5
|
8.0
|
1.0
|
|
CHD
|
B:HEM200
|
3.5
|
14.4
|
0.5
|
|
CHB
|
B:HEM200
|
3.5
|
12.5
|
0.5
|
|
CG
|
A:MET52
|
3.5
|
6.0
|
1.0
|
|
CHB
|
A:HEM200
|
3.5
|
5.3
|
0.5
|
|
CHA
|
A:HEM200
|
3.5
|
5.0
|
0.5
|
|
C3C
|
A:HEM200
|
4.1
|
10.2
|
0.5
|
|
C2C
|
A:HEM200
|
4.1
|
8.3
|
0.5
|
|
CB
|
B:MET52
|
4.1
|
7.2
|
1.0
|
|
C2D
|
A:HEM200
|
4.2
|
6.7
|
0.5
|
|
C2C
|
B:HEM200
|
4.3
|
13.9
|
0.5
|
|
C3B
|
A:HEM200
|
4.3
|
8.0
|
0.5
|
|
C3D
|
A:HEM200
|
4.3
|
7.7
|
0.5
|
|
CB
|
A:MET52
|
4.3
|
7.6
|
1.0
|
|
C2B
|
A:HEM200
|
4.3
|
5.8
|
0.5
|
|
C2A
|
B:HEM200
|
4.3
|
13.1
|
0.5
|
|
C3D
|
B:HEM200
|
4.3
|
14.3
|
0.5
|
|
C3A
|
B:HEM200
|
4.3
|
10.4
|
0.5
|
|
C2D
|
B:HEM200
|
4.3
|
13.8
|
0.5
|
|
C3B
|
B:HEM200
|
4.3
|
13.1
|
0.5
|
|
C3C
|
B:HEM200
|
4.3
|
15.9
|
0.5
|
|
C2B
|
B:HEM200
|
4.3
|
11.9
|
0.5
|
|
C3A
|
A:HEM200
|
4.4
|
4.0
|
0.5
|
|
C2A
|
A:HEM200
|
4.4
|
5.7
|
0.5
|
|
Iron binding site 3 out
of 12 in 2y3q
Go back to
Iron Binding Sites List in 2y3q
Iron binding site 3 out
of 12 in the 1.55A Structure of Apo Bacterioferritin From E. Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of 1.55A Structure of Apo Bacterioferritin From E. Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe200
b:4.0
occ:0.45
|
FE
|
C:HEM200
|
0.0
|
4.0
|
0.5
|
|
FE
|
D:HEM200
|
0.1
|
18.9
|
0.5
|
|
NC
|
C:HEM200
|
2.0
|
4.8
|
0.5
|
|
ND
|
C:HEM200
|
2.0
|
3.8
|
0.5
|
|
ND
|
D:HEM200
|
2.0
|
18.8
|
0.5
|
|
NA
|
C:HEM200
|
2.0
|
4.3
|
0.5
|
|
NB
|
C:HEM200
|
2.0
|
4.6
|
0.5
|
|
NA
|
D:HEM200
|
2.1
|
18.6
|
0.5
|
|
NB
|
D:HEM200
|
2.1
|
18.8
|
0.5
|
|
NC
|
D:HEM200
|
2.1
|
18.4
|
0.5
|
|
SD
|
D:MET52
|
2.3
|
9.1
|
1.0
|
|
SD
|
C:MET52
|
2.3
|
9.0
|
1.0
|
|
C4C
|
C:HEM200
|
3.0
|
5.2
|
0.5
|
|
C4D
|
D:HEM200
|
3.0
|
18.5
|
0.5
|
|
C1D
|
D:HEM200
|
3.0
|
18.2
|
0.5
|
|
C4D
|
C:HEM200
|
3.0
|
3.8
|
0.5
|
|
C1D
|
C:HEM200
|
3.0
|
5.5
|
0.5
|
|
C1A
|
C:HEM200
|
3.0
|
3.4
|
0.5
|
|
C1B
|
C:HEM200
|
3.0
|
5.1
|
0.5
|
|
C1C
|
C:HEM200
|
3.0
|
5.0
|
0.5
|
|
C4A
|
C:HEM200
|
3.0
|
2.9
|
0.5
|
|
C1A
|
D:HEM200
|
3.1
|
18.4
|
0.5
|
|
C4B
|
C:HEM200
|
3.1
|
5.7
|
0.5
|
|
C1B
|
D:HEM200
|
3.1
|
17.9
|
0.5
|
|
C4C
|
D:HEM200
|
3.1
|
18.8
|
0.5
|
|
C4A
|
D:HEM200
|
3.1
|
18.6
|
0.5
|
|
C4B
|
D:HEM200
|
3.1
|
18.1
|
0.5
|
|
C1C
|
D:HEM200
|
3.2
|
18.1
|
0.5
|
|
CE
|
C:MET52
|
3.2
|
10.1
|
1.0
|
|
CE
|
D:MET52
|
3.3
|
8.6
|
1.0
|
|
CHD
|
C:HEM200
|
3.4
|
6.0
|
0.5
|
|
CHA
|
D:HEM200
|
3.4
|
18.6
|
0.5
|
|
CHA
|
C:HEM200
|
3.4
|
2.8
|
0.5
|
|
CHD
|
D:HEM200
|
3.4
|
19.0
|
0.5
|
|
CHB
|
C:HEM200
|
3.4
|
3.9
|
0.5
|
|
CHC
|
C:HEM200
|
3.5
|
5.7
|
0.5
|
|
CG
|
C:MET52
|
3.5
|
6.8
|
1.0
|
|
CHB
|
D:HEM200
|
3.5
|
18.1
|
0.5
|
|
CG
|
D:MET52
|
3.5
|
8.6
|
1.0
|
|
CHC
|
D:HEM200
|
3.5
|
18.3
|
0.5
|
|
C3D
|
D:HEM200
|
4.2
|
19.1
|
0.5
|
|
CB
|
D:MET52
|
4.2
|
6.8
|
1.0
|
|
C3C
|
C:HEM200
|
4.2
|
8.9
|
0.5
|
|
C2D
|
D:HEM200
|
4.2
|
18.0
|
0.5
|
|
CB
|
C:MET52
|
4.2
|
7.0
|
1.0
|
|
C2C
|
C:HEM200
|
4.2
|
6.8
|
0.5
|
|
C2D
|
C:HEM200
|
4.2
|
6.4
|
0.5
|
|
C2A
|
C:HEM200
|
4.2
|
5.4
|
0.5
|
|
C3D
|
C:HEM200
|
4.3
|
6.2
|
0.5
|
|
C3A
|
C:HEM200
|
4.3
|
4.4
|
0.5
|
|
C2B
|
C:HEM200
|
4.3
|
4.5
|
0.5
|
|
C3B
|
C:HEM200
|
4.3
|
4.9
|
0.5
|
|
C2A
|
D:HEM200
|
4.3
|
18.8
|
0.5
|
|
C2B
|
D:HEM200
|
4.3
|
18.0
|
0.5
|
|
C3A
|
D:HEM200
|
4.3
|
18.8
|
0.5
|
|
C3B
|
D:HEM200
|
4.3
|
17.8
|
0.5
|
|
C3C
|
D:HEM200
|
4.3
|
18.7
|
0.5
|
|
C2C
|
D:HEM200
|
4.4
|
17.7
|
0.5
|
|
Iron binding site 4 out
of 12 in 2y3q
Go back to
Iron Binding Sites List in 2y3q
Iron binding site 4 out
of 12 in the 1.55A Structure of Apo Bacterioferritin From E. Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of 1.55A Structure of Apo Bacterioferritin From E. Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe200
b:18.9
occ:0.45
|
FE
|
D:HEM200
|
0.0
|
18.9
|
0.5
|
|
FE
|
C:HEM200
|
0.1
|
4.0
|
0.5
|
|
NB
|
C:HEM200
|
1.9
|
4.6
|
0.5
|
|
NC
|
C:HEM200
|
2.0
|
4.8
|
0.5
|
|
ND
|
D:HEM200
|
2.0
|
18.8
|
0.5
|
|
NC
|
D:HEM200
|
2.0
|
18.4
|
0.5
|
|
NA
|
C:HEM200
|
2.0
|
4.3
|
0.5
|
|
NB
|
D:HEM200
|
2.1
|
18.8
|
0.5
|
|
ND
|
C:HEM200
|
2.1
|
3.8
|
0.5
|
|
NA
|
D:HEM200
|
2.2
|
18.6
|
0.5
|
|
SD
|
C:MET52
|
2.3
|
9.0
|
1.0
|
|
SD
|
D:MET52
|
2.3
|
9.1
|
1.0
|
|
C1B
|
C:HEM200
|
2.9
|
5.1
|
0.5
|
|
C1D
|
D:HEM200
|
3.0
|
18.2
|
0.5
|
|
C4B
|
C:HEM200
|
3.0
|
5.7
|
0.5
|
|
C4C
|
D:HEM200
|
3.0
|
18.8
|
0.5
|
|
C1C
|
C:HEM200
|
3.0
|
5.0
|
0.5
|
|
C4A
|
C:HEM200
|
3.0
|
2.9
|
0.5
|
|
C4D
|
D:HEM200
|
3.0
|
18.5
|
0.5
|
|
C4C
|
C:HEM200
|
3.0
|
5.2
|
0.5
|
|
C1C
|
D:HEM200
|
3.1
|
18.1
|
0.5
|
|
C1A
|
C:HEM200
|
3.1
|
3.4
|
0.5
|
|
C4B
|
D:HEM200
|
3.1
|
18.1
|
0.5
|
|
CE
|
C:MET52
|
3.1
|
10.1
|
1.0
|
|
C1D
|
C:HEM200
|
3.1
|
5.5
|
0.5
|
|
C4D
|
C:HEM200
|
3.1
|
3.8
|
0.5
|
|
C1B
|
D:HEM200
|
3.2
|
17.9
|
0.5
|
|
C1A
|
D:HEM200
|
3.2
|
18.4
|
0.5
|
|
C4A
|
D:HEM200
|
3.2
|
18.6
|
0.5
|
|
CHD
|
D:HEM200
|
3.3
|
19.0
|
0.5
|
|
CHB
|
C:HEM200
|
3.3
|
3.9
|
0.5
|
|
CE
|
D:MET52
|
3.4
|
8.6
|
1.0
|
|
CHC
|
C:HEM200
|
3.4
|
5.7
|
0.5
|
|
CG
|
C:MET52
|
3.4
|
6.8
|
1.0
|
|
CHC
|
D:HEM200
|
3.4
|
18.3
|
0.5
|
|
CHA
|
D:HEM200
|
3.5
|
18.6
|
0.5
|
|
CHD
|
C:HEM200
|
3.5
|
6.0
|
0.5
|
|
CG
|
D:MET52
|
3.5
|
8.6
|
1.0
|
|
CHA
|
C:HEM200
|
3.5
|
2.8
|
0.5
|
|
CHB
|
D:HEM200
|
3.6
|
18.1
|
0.5
|
|
C2B
|
C:HEM200
|
4.1
|
4.5
|
0.5
|
|
C3B
|
C:HEM200
|
4.2
|
4.9
|
0.5
|
|
C2D
|
D:HEM200
|
4.2
|
18.0
|
0.5
|
|
CB
|
D:MET52
|
4.2
|
6.8
|
1.0
|
|
C2C
|
C:HEM200
|
4.2
|
6.8
|
0.5
|
|
C3D
|
D:HEM200
|
4.2
|
19.1
|
0.5
|
|
C3C
|
D:HEM200
|
4.2
|
18.7
|
0.5
|
|
C3C
|
C:HEM200
|
4.2
|
8.9
|
0.5
|
|
CB
|
C:MET52
|
4.2
|
7.0
|
1.0
|
|
C2C
|
D:HEM200
|
4.2
|
17.7
|
0.5
|
|
C3A
|
C:HEM200
|
4.3
|
4.4
|
0.5
|
|
C2A
|
C:HEM200
|
4.3
|
5.4
|
0.5
|
|
C3B
|
D:HEM200
|
4.3
|
17.8
|
0.5
|
|
C2B
|
D:HEM200
|
4.4
|
18.0
|
0.5
|
|
C2D
|
C:HEM200
|
4.4
|
6.4
|
0.5
|
|
C3D
|
C:HEM200
|
4.4
|
6.2
|
0.5
|
|
C2A
|
D:HEM200
|
4.4
|
18.8
|
0.5
|
|
C3A
|
D:HEM200
|
4.4
|
18.8
|
0.5
|
|
Iron binding site 5 out
of 12 in 2y3q
Go back to
Iron Binding Sites List in 2y3q
Iron binding site 5 out
of 12 in the 1.55A Structure of Apo Bacterioferritin From E. Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of 1.55A Structure of Apo Bacterioferritin From E. Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe200
b:6.7
occ:0.45
|
FE
|
E:HEM200
|
0.0
|
6.7
|
0.5
|
|
FE
|
F:HEM200
|
0.3
|
11.2
|
0.5
|
|
ND
|
F:HEM200
|
1.9
|
10.9
|
0.5
|
|
NA
|
E:HEM200
|
2.0
|
5.7
|
0.5
|
|
NA
|
F:HEM200
|
2.0
|
10.7
|
0.5
|
|
ND
|
E:HEM200
|
2.0
|
6.2
|
0.5
|
|
NC
|
E:HEM200
|
2.1
|
7.0
|
0.5
|
|
NC
|
F:HEM200
|
2.1
|
9.6
|
0.5
|
|
NB
|
E:HEM200
|
2.1
|
6.7
|
0.5
|
|
NB
|
F:HEM200
|
2.2
|
9.9
|
0.5
|
|
SD
|
F:MET52
|
2.3
|
9.2
|
1.0
|
|
SD
|
E:MET52
|
2.3
|
8.9
|
1.0
|
|
C1D
|
F:HEM200
|
2.9
|
10.8
|
0.5
|
|
C4D
|
F:HEM200
|
2.9
|
11.4
|
0.5
|
|
C1A
|
F:HEM200
|
3.0
|
11.2
|
0.5
|
|
C4C
|
F:HEM200
|
3.0
|
11.0
|
0.5
|
|
C4A
|
E:HEM200
|
3.0
|
7.6
|
0.5
|
|
C1D
|
E:HEM200
|
3.0
|
5.8
|
0.5
|
|
C4D
|
E:HEM200
|
3.0
|
6.4
|
0.5
|
|
C1A
|
E:HEM200
|
3.0
|
5.6
|
0.5
|
|
C1B
|
E:HEM200
|
3.1
|
7.0
|
0.5
|
|
C4C
|
E:HEM200
|
3.1
|
6.4
|
0.5
|
|
C1C
|
E:HEM200
|
3.1
|
6.5
|
0.5
|
|
C4A
|
F:HEM200
|
3.1
|
10.6
|
0.5
|
|
C4B
|
E:HEM200
|
3.1
|
8.1
|
0.5
|
|
C1C
|
F:HEM200
|
3.2
|
11.0
|
0.5
|
|
C1B
|
F:HEM200
|
3.2
|
9.4
|
0.5
|
|
C4B
|
F:HEM200
|
3.3
|
10.0
|
0.5
|
|
CE
|
E:MET52
|
3.3
|
9.2
|
1.0
|
|
CHD
|
F:HEM200
|
3.3
|
10.6
|
0.5
|
|
CHA
|
F:HEM200
|
3.3
|
11.7
|
0.5
|
|
CE
|
F:MET52
|
3.4
|
11.4
|
1.0
|
|
CHB
|
E:HEM200
|
3.4
|
7.2
|
0.5
|
|
CHA
|
E:HEM200
|
3.4
|
6.5
|
0.5
|
|
CHD
|
E:HEM200
|
3.4
|
6.5
|
0.5
|
|
CG
|
F:MET52
|
3.4
|
7.4
|
1.0
|
|
CHC
|
E:HEM200
|
3.5
|
8.4
|
0.5
|
|
CHB
|
F:HEM200
|
3.6
|
10.8
|
0.5
|
|
CG
|
E:MET52
|
3.6
|
8.4
|
1.0
|
|
CHC
|
F:HEM200
|
3.6
|
9.9
|
0.5
|
|
C3D
|
F:HEM200
|
4.1
|
12.1
|
0.5
|
|
C2D
|
F:HEM200
|
4.1
|
10.6
|
0.5
|
|
CB
|
F:MET52
|
4.2
|
7.0
|
1.0
|
|
C3A
|
E:HEM200
|
4.2
|
6.5
|
0.5
|
|
C2A
|
F:HEM200
|
4.2
|
11.7
|
0.5
|
|
C2A
|
E:HEM200
|
4.2
|
6.1
|
0.5
|
|
C2D
|
E:HEM200
|
4.2
|
7.4
|
0.5
|
|
C3D
|
E:HEM200
|
4.3
|
6.9
|
0.5
|
|
C3C
|
F:HEM200
|
4.3
|
11.7
|
0.5
|
|
CB
|
E:MET52
|
4.3
|
7.1
|
1.0
|
|
C3A
|
F:HEM200
|
4.3
|
11.3
|
0.5
|
|
C2B
|
E:HEM200
|
4.3
|
7.5
|
0.5
|
|
C3C
|
E:HEM200
|
4.3
|
8.5
|
0.5
|
|
C2C
|
E:HEM200
|
4.3
|
7.5
|
0.5
|
|
C2C
|
F:HEM200
|
4.3
|
10.4
|
0.5
|
|
C3B
|
E:HEM200
|
4.3
|
8.5
|
0.5
|
|
C2B
|
F:HEM200
|
4.5
|
8.8
|
0.5
|
|
C3B
|
F:HEM200
|
4.5
|
8.8
|
0.5
|
|
Iron binding site 6 out
of 12 in 2y3q
Go back to
Iron Binding Sites List in 2y3q
Iron binding site 6 out
of 12 in the 1.55A Structure of Apo Bacterioferritin From E. Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of 1.55A Structure of Apo Bacterioferritin From E. Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe200
b:11.2
occ:0.45
|
FE
|
F:HEM200
|
0.0
|
11.2
|
0.5
|
|
FE
|
E:HEM200
|
0.3
|
6.7
|
0.5
|
|
NC
|
E:HEM200
|
1.8
|
7.0
|
0.5
|
|
NB
|
F:HEM200
|
2.0
|
9.9
|
0.5
|
|
NC
|
F:HEM200
|
2.0
|
9.6
|
0.5
|
|
NB
|
E:HEM200
|
2.1
|
6.7
|
0.5
|
|
NA
|
F:HEM200
|
2.1
|
10.7
|
0.5
|
|
ND
|
E:HEM200
|
2.1
|
6.2
|
0.5
|
|
ND
|
F:HEM200
|
2.1
|
10.9
|
0.5
|
|
NA
|
E:HEM200
|
2.3
|
5.7
|
0.5
|
|
SD
|
E:MET52
|
2.3
|
8.9
|
1.0
|
|
SD
|
F:MET52
|
2.4
|
9.2
|
1.0
|
|
C4C
|
E:HEM200
|
2.8
|
6.4
|
0.5
|
|
C1C
|
E:HEM200
|
2.8
|
6.5
|
0.5
|
|
C1D
|
E:HEM200
|
3.0
|
5.8
|
0.5
|
|
C4B
|
F:HEM200
|
3.0
|
10.0
|
0.5
|
|
C1C
|
F:HEM200
|
3.0
|
11.0
|
0.5
|
|
C1B
|
F:HEM200
|
3.0
|
9.4
|
0.5
|
|
C4B
|
E:HEM200
|
3.0
|
8.1
|
0.5
|
|
C4C
|
F:HEM200
|
3.0
|
11.0
|
0.5
|
|
C4A
|
F:HEM200
|
3.1
|
10.6
|
0.5
|
|
C1D
|
F:HEM200
|
3.1
|
10.8
|
0.5
|
|
C1A
|
F:HEM200
|
3.1
|
11.2
|
0.5
|
|
C1B
|
E:HEM200
|
3.1
|
7.0
|
0.5
|
|
C4D
|
F:HEM200
|
3.2
|
11.4
|
0.5
|
|
C4D
|
E:HEM200
|
3.2
|
6.4
|
0.5
|
|
CHD
|
E:HEM200
|
3.2
|
6.5
|
0.5
|
|
C4A
|
E:HEM200
|
3.3
|
7.6
|
0.5
|
|
CE
|
E:MET52
|
3.3
|
9.2
|
1.0
|
|
CHC
|
E:HEM200
|
3.3
|
8.4
|
0.5
|
|
C1A
|
E:HEM200
|
3.3
|
5.6
|
0.5
|
|
CE
|
F:MET52
|
3.3
|
11.4
|
1.0
|
|
CHC
|
F:HEM200
|
3.4
|
9.9
|
0.5
|
|
CG
|
E:MET52
|
3.4
|
8.4
|
1.0
|
|
CHB
|
F:HEM200
|
3.4
|
10.8
|
0.5
|
|
CHD
|
F:HEM200
|
3.4
|
10.6
|
0.5
|
|
CG
|
F:MET52
|
3.5
|
7.4
|
1.0
|
|
CHA
|
F:HEM200
|
3.5
|
11.7
|
0.5
|
|
CHB
|
E:HEM200
|
3.6
|
7.2
|
0.5
|
|
CHA
|
E:HEM200
|
3.6
|
6.5
|
0.5
|
|
C2C
|
E:HEM200
|
4.0
|
7.5
|
0.5
|
|
C3C
|
E:HEM200
|
4.0
|
8.5
|
0.5
|
|
CB
|
E:MET52
|
4.1
|
7.1
|
1.0
|
|
C3B
|
F:HEM200
|
4.2
|
8.8
|
0.5
|
|
C2B
|
F:HEM200
|
4.2
|
8.8
|
0.5
|
|
C2C
|
F:HEM200
|
4.2
|
10.4
|
0.5
|
|
C2D
|
E:HEM200
|
4.2
|
7.4
|
0.5
|
|
C3C
|
F:HEM200
|
4.2
|
11.7
|
0.5
|
|
C3B
|
E:HEM200
|
4.3
|
8.5
|
0.5
|
|
C3A
|
F:HEM200
|
4.3
|
11.3
|
0.5
|
|
C2B
|
E:HEM200
|
4.3
|
7.5
|
0.5
|
|
C2A
|
F:HEM200
|
4.3
|
11.7
|
0.5
|
|
CB
|
F:MET52
|
4.3
|
7.0
|
1.0
|
|
C3D
|
E:HEM200
|
4.3
|
6.9
|
0.5
|
|
C2D
|
F:HEM200
|
4.4
|
10.6
|
0.5
|
|
C3D
|
F:HEM200
|
4.4
|
12.1
|
0.5
|
|
C3A
|
E:HEM200
|
4.5
|
6.5
|
0.5
|
|
C2A
|
E:HEM200
|
4.5
|
6.1
|
0.5
|
|
Iron binding site 7 out
of 12 in 2y3q
Go back to
Iron Binding Sites List in 2y3q
Iron binding site 7 out
of 12 in the 1.55A Structure of Apo Bacterioferritin From E. Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of 1.55A Structure of Apo Bacterioferritin From E. Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Fe200
b:15.4
occ:0.45
|
FE
|
G:HEM200
|
0.0
|
15.4
|
0.5
|
|
FE
|
H:HEM200
|
0.2
|
5.6
|
0.5
|
|
ND
|
H:HEM200
|
1.8
|
5.6
|
0.5
|
|
NA
|
G:HEM200
|
2.0
|
14.0
|
0.5
|
|
NA
|
H:HEM200
|
2.0
|
6.3
|
0.5
|
|
ND
|
G:HEM200
|
2.0
|
16.0
|
0.5
|
|
NB
|
G:HEM200
|
2.1
|
13.5
|
0.5
|
|
NC
|
H:HEM200
|
2.1
|
5.2
|
0.5
|
|
NC
|
G:HEM200
|
2.1
|
14.9
|
0.5
|
|
NB
|
H:HEM200
|
2.2
|
4.3
|
0.5
|
|
SD
|
H:MET52
|
2.3
|
9.5
|
1.0
|
|
SD
|
G:MET52
|
2.3
|
9.0
|
1.0
|
|
C1D
|
H:HEM200
|
2.8
|
4.9
|
0.5
|
|
C4D
|
H:HEM200
|
2.8
|
4.0
|
0.5
|
|
C1A
|
G:HEM200
|
3.0
|
13.9
|
0.5
|
|
C1A
|
H:HEM200
|
3.0
|
5.5
|
0.5
|
|
C4D
|
G:HEM200
|
3.0
|
14.8
|
0.5
|
|
C4C
|
H:HEM200
|
3.0
|
7.5
|
0.5
|
|
C4A
|
G:HEM200
|
3.0
|
12.7
|
0.5
|
|
C1D
|
G:HEM200
|
3.0
|
15.3
|
0.5
|
|
C4A
|
H:HEM200
|
3.1
|
5.2
|
0.5
|
|
C1B
|
G:HEM200
|
3.1
|
12.0
|
0.5
|
|
C4C
|
G:HEM200
|
3.1
|
16.5
|
0.5
|
|
C4B
|
G:HEM200
|
3.2
|
13.3
|
0.5
|
|
C1C
|
G:HEM200
|
3.2
|
15.2
|
0.5
|
|
C1B
|
H:HEM200
|
3.2
|
5.2
|
0.5
|
|
CHD
|
H:HEM200
|
3.2
|
5.8
|
0.5
|
|
C1C
|
H:HEM200
|
3.2
|
7.5
|
0.5
|
|
CHA
|
H:HEM200
|
3.3
|
3.2
|
0.5
|
|
CE
|
G:MET52
|
3.3
|
11.3
|
1.0
|
|
CHA
|
G:HEM200
|
3.3
|
13.4
|
0.5
|
|
C4B
|
H:HEM200
|
3.3
|
6.7
|
0.5
|
|
CE
|
H:MET52
|
3.3
|
9.6
|
1.0
|
|
CHB
|
G:HEM200
|
3.4
|
12.7
|
0.5
|
|
CHD
|
G:HEM200
|
3.4
|
16.2
|
0.5
|
|
CG
|
H:MET52
|
3.5
|
8.5
|
1.0
|
|
CHB
|
H:HEM200
|
3.5
|
6.1
|
0.5
|
|
CG
|
G:MET52
|
3.6
|
7.1
|
1.0
|
|
CHC
|
G:HEM200
|
3.6
|
15.1
|
0.5
|
|
CHC
|
H:HEM200
|
3.7
|
8.0
|
0.5
|
|
C2D
|
H:HEM200
|
4.0
|
5.0
|
0.5
|
|
C3D
|
H:HEM200
|
4.0
|
4.8
|
0.5
|
|
CB
|
H:MET52
|
4.1
|
7.7
|
1.0
|
|
C2A
|
G:HEM200
|
4.2
|
14.3
|
0.5
|
|
C3A
|
G:HEM200
|
4.2
|
11.1
|
0.5
|
|
C2A
|
H:HEM200
|
4.2
|
6.8
|
0.5
|
|
C3D
|
G:HEM200
|
4.2
|
15.5
|
0.5
|
|
C2D
|
G:HEM200
|
4.3
|
15.6
|
0.5
|
|
C3C
|
H:HEM200
|
4.3
|
9.4
|
0.5
|
|
C3A
|
H:HEM200
|
4.3
|
6.4
|
0.5
|
|
CB
|
G:MET52
|
4.3
|
7.1
|
1.0
|
|
C2B
|
G:HEM200
|
4.3
|
11.6
|
0.5
|
|
C3B
|
G:HEM200
|
4.4
|
11.8
|
0.5
|
|
C2C
|
H:HEM200
|
4.4
|
7.4
|
0.5
|
|
C3C
|
G:HEM200
|
4.4
|
17.7
|
0.5
|
|
C2C
|
G:HEM200
|
4.4
|
15.9
|
0.5
|
|
C2B
|
H:HEM200
|
4.5
|
4.2
|
0.5
|
|
C3B
|
H:HEM200
|
4.5
|
4.9
|
0.5
|
|
Iron binding site 8 out
of 12 in 2y3q
Go back to
Iron Binding Sites List in 2y3q
Iron binding site 8 out
of 12 in the 1.55A Structure of Apo Bacterioferritin From E. Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of 1.55A Structure of Apo Bacterioferritin From E. Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Fe200
b:5.6
occ:0.45
|
FE
|
H:HEM200
|
0.0
|
5.6
|
0.5
|
|
FE
|
G:HEM200
|
0.2
|
15.4
|
0.5
|
|
NC
|
G:HEM200
|
1.9
|
14.9
|
0.5
|
|
NB
|
H:HEM200
|
2.0
|
4.3
|
0.5
|
|
NA
|
H:HEM200
|
2.0
|
6.3
|
0.5
|
|
ND
|
G:HEM200
|
2.0
|
16.0
|
0.5
|
|
ND
|
H:HEM200
|
2.0
|
5.6
|
0.5
|
|
NC
|
H:HEM200
|
2.0
|
5.2
|
0.5
|
|
NB
|
G:HEM200
|
2.1
|
13.5
|
0.5
|
|
NA
|
G:HEM200
|
2.2
|
14.0
|
0.5
|
|
SD
|
G:MET52
|
2.3
|
9.0
|
1.0
|
|
SD
|
H:MET52
|
2.3
|
9.5
|
1.0
|
|
C4C
|
G:HEM200
|
2.9
|
16.5
|
0.5
|
|
C1D
|
G:HEM200
|
3.0
|
15.3
|
0.5
|
|
C1C
|
G:HEM200
|
3.0
|
15.2
|
0.5
|
|
C1D
|
H:HEM200
|
3.0
|
4.9
|
0.5
|
|
C1B
|
H:HEM200
|
3.0
|
5.2
|
0.5
|
|
C4C
|
H:HEM200
|
3.0
|
7.5
|
0.5
|
|
C4A
|
H:HEM200
|
3.0
|
5.2
|
0.5
|
|
C4D
|
H:HEM200
|
3.1
|
4.0
|
0.5
|
|
C1A
|
H:HEM200
|
3.1
|
5.5
|
0.5
|
|
C4B
|
G:HEM200
|
3.1
|
13.3
|
0.5
|
|
C4D
|
G:HEM200
|
3.1
|
14.8
|
0.5
|
|
C1C
|
H:HEM200
|
3.1
|
7.5
|
0.5
|
|
C4B
|
H:HEM200
|
3.1
|
6.7
|
0.5
|
|
C1B
|
G:HEM200
|
3.2
|
12.0
|
0.5
|
|
C1A
|
G:HEM200
|
3.2
|
13.9
|
0.5
|
|
C4A
|
G:HEM200
|
3.2
|
12.7
|
0.5
|
|
CE
|
H:MET52
|
3.3
|
9.6
|
1.0
|
|
CHD
|
G:HEM200
|
3.3
|
16.2
|
0.5
|
|
CE
|
G:MET52
|
3.3
|
11.3
|
1.0
|
|
CHD
|
H:HEM200
|
3.4
|
5.8
|
0.5
|
|
CHB
|
H:HEM200
|
3.4
|
6.1
|
0.5
|
|
CHC
|
G:HEM200
|
3.4
|
15.1
|
0.5
|
|
CG
|
G:MET52
|
3.4
|
7.1
|
1.0
|
|
CHA
|
H:HEM200
|
3.4
|
3.2
|
0.5
|
|
CHA
|
G:HEM200
|
3.5
|
13.4
|
0.5
|
|
CG
|
H:MET52
|
3.5
|
8.5
|
1.0
|
|
CHC
|
H:HEM200
|
3.5
|
8.0
|
0.5
|
|
CHB
|
G:HEM200
|
3.6
|
12.7
|
0.5
|
|
C3C
|
G:HEM200
|
4.2
|
17.7
|
0.5
|
|
C2C
|
G:HEM200
|
4.2
|
15.9
|
0.5
|
|
CB
|
G:MET52
|
4.2
|
7.1
|
1.0
|
|
C2D
|
G:HEM200
|
4.2
|
15.6
|
0.5
|
|
C2D
|
H:HEM200
|
4.2
|
5.0
|
0.5
|
|
CB
|
H:MET52
|
4.2
|
7.7
|
1.0
|
|
C2B
|
H:HEM200
|
4.2
|
4.2
|
0.5
|
|
C3C
|
H:HEM200
|
4.3
|
9.4
|
0.5
|
|
C3D
|
H:HEM200
|
4.3
|
4.8
|
0.5
|
|
C2A
|
H:HEM200
|
4.3
|
6.8
|
0.5
|
|
C3A
|
H:HEM200
|
4.3
|
6.4
|
0.5
|
|
C3D
|
G:HEM200
|
4.3
|
15.5
|
0.5
|
|
C2C
|
H:HEM200
|
4.3
|
7.4
|
0.5
|
|
C3B
|
H:HEM200
|
4.3
|
4.9
|
0.5
|
|
C3B
|
G:HEM200
|
4.3
|
11.8
|
0.5
|
|
C2B
|
G:HEM200
|
4.4
|
11.6
|
0.5
|
|
C2A
|
G:HEM200
|
4.4
|
14.3
|
0.5
|
|
C3A
|
G:HEM200
|
4.4
|
11.1
|
0.5
|
|
Iron binding site 9 out
of 12 in 2y3q
Go back to
Iron Binding Sites List in 2y3q
Iron binding site 9 out
of 12 in the 1.55A Structure of Apo Bacterioferritin From E. Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of 1.55A Structure of Apo Bacterioferritin From E. Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Fe200
b:15.5
occ:0.45
|
FE
|
I:HEM200
|
0.0
|
15.5
|
0.5
|
|
FE
|
J:HEM200
|
0.3
|
4.8
|
0.5
|
|
ND
|
I:HEM200
|
2.0
|
14.8
|
0.5
|
|
NA
|
J:HEM200
|
2.0
|
5.1
|
0.5
|
|
NC
|
J:HEM200
|
2.0
|
5.9
|
0.5
|
|
NB
|
J:HEM200
|
2.0
|
5.4
|
0.5
|
|
ND
|
J:HEM200
|
2.0
|
6.9
|
0.5
|
|
NC
|
I:HEM200
|
2.0
|
14.9
|
0.5
|
|
NA
|
I:HEM200
|
2.1
|
13.6
|
0.5
|
|
NB
|
I:HEM200
|
2.1
|
13.1
|
0.5
|
|
SD
|
J:MET52
|
2.1
|
9.0
|
1.0
|
|
SD
|
I:MET52
|
2.5
|
9.3
|
1.0
|
|
C4D
|
I:HEM200
|
3.0
|
14.7
|
0.5
|
|
C1D
|
I:HEM200
|
3.0
|
15.5
|
0.5
|
|
C4C
|
J:HEM200
|
3.0
|
9.5
|
0.5
|
|
C1D
|
J:HEM200
|
3.0
|
8.2
|
0.5
|
|
C1A
|
I:HEM200
|
3.0
|
13.1
|
0.5
|
|
C1B
|
J:HEM200
|
3.0
|
6.2
|
0.5
|
|
C4A
|
J:HEM200
|
3.0
|
5.5
|
0.5
|
|
C1A
|
J:HEM200
|
3.1
|
6.1
|
0.5
|
|
C4C
|
I:HEM200
|
3.1
|
16.0
|
0.5
|
|
C4D
|
J:HEM200
|
3.1
|
7.7
|
0.5
|
|
C1C
|
J:HEM200
|
3.1
|
8.8
|
0.5
|
|
CE
|
J:MET52
|
3.1
|
10.6
|
1.0
|
|
C1C
|
I:HEM200
|
3.1
|
14.5
|
0.5
|
|
C4B
|
J:HEM200
|
3.1
|
6.8
|
0.5
|
|
C4A
|
I:HEM200
|
3.1
|
12.1
|
0.5
|
|
C4B
|
I:HEM200
|
3.1
|
13.6
|
0.5
|
|
C1B
|
I:HEM200
|
3.1
|
12.8
|
0.5
|
|
CG
|
J:MET52
|
3.3
|
6.9
|
1.0
|
|
CHA
|
I:HEM200
|
3.3
|
14.0
|
0.5
|
|
CHD
|
J:HEM200
|
3.4
|
9.0
|
0.5
|
|
CHD
|
I:HEM200
|
3.4
|
15.6
|
0.5
|
|
CHB
|
J:HEM200
|
3.4
|
5.9
|
0.5
|
|
CHA
|
J:HEM200
|
3.4
|
7.2
|
0.5
|
|
CE
|
I:MET52
|
3.5
|
9.5
|
1.0
|
|
CHC
|
I:HEM200
|
3.5
|
13.7
|
0.5
|
|
CHC
|
J:HEM200
|
3.5
|
8.4
|
0.5
|
|
CHB
|
I:HEM200
|
3.5
|
12.5
|
0.5
|
|
CG
|
I:MET52
|
3.6
|
7.0
|
1.0
|
|
CB
|
J:MET52
|
4.1
|
7.1
|
1.0
|
|
C3D
|
I:HEM200
|
4.2
|
15.7
|
0.5
|
|
C2D
|
I:HEM200
|
4.2
|
15.8
|
0.5
|
|
C3C
|
J:HEM200
|
4.2
|
12.0
|
0.5
|
|
C2D
|
J:HEM200
|
4.2
|
9.1
|
0.5
|
|
C2B
|
J:HEM200
|
4.2
|
7.2
|
0.5
|
|
C2A
|
I:HEM200
|
4.3
|
12.6
|
0.5
|
|
C3A
|
J:HEM200
|
4.3
|
5.9
|
0.5
|
|
C3D
|
J:HEM200
|
4.3
|
9.4
|
0.5
|
|
C2A
|
J:HEM200
|
4.3
|
7.0
|
0.5
|
|
C2C
|
J:HEM200
|
4.3
|
10.5
|
0.5
|
|
C3C
|
I:HEM200
|
4.3
|
16.4
|
0.5
|
|
C3B
|
J:HEM200
|
4.3
|
8.0
|
0.5
|
|
C3A
|
I:HEM200
|
4.3
|
11.5
|
0.5
|
|
C2C
|
I:HEM200
|
4.3
|
14.2
|
0.5
|
|
CB
|
I:MET52
|
4.3
|
7.4
|
1.0
|
|
C3B
|
I:HEM200
|
4.4
|
13.0
|
0.5
|
|
C2B
|
I:HEM200
|
4.4
|
12.4
|
0.5
|
|
Iron binding site 10 out
of 12 in 2y3q
Go back to
Iron Binding Sites List in 2y3q
Iron binding site 10 out
of 12 in the 1.55A Structure of Apo Bacterioferritin From E. Coli
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of 1.55A Structure of Apo Bacterioferritin From E. Coli within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Fe200
b:4.8
occ:0.45
|
FE
|
J:HEM200
|
0.0
|
4.8
|
0.5
|
|
FE
|
I:HEM200
|
0.3
|
15.5
|
0.5
|
|
NC
|
J:HEM200
|
2.0
|
5.9
|
0.5
|
|
ND
|
I:HEM200
|
2.0
|
14.8
|
0.5
|
|
NA
|
J:HEM200
|
2.0
|
5.1
|
0.5
|
|
ND
|
J:HEM200
|
2.0
|
6.9
|
0.5
|
|
NA
|
I:HEM200
|
2.0
|
13.6
|
0.5
|
|
NB
|
J:HEM200
|
2.0
|
5.4
|
0.5
|
|
NC
|
I:HEM200
|
2.1
|
14.9
|
0.5
|
|
NB
|
I:HEM200
|
2.1
|
13.1
|
0.5
|
|
SD
|
I:MET52
|
2.2
|
9.3
|
1.0
|
|
SD
|
J:MET52
|
2.4
|
9.0
|
1.0
|
|
C4D
|
I:HEM200
|
3.0
|
14.7
|
0.5
|
|
C4C
|
J:HEM200
|
3.0
|
9.5
|
0.5
|
|
C1D
|
I:HEM200
|
3.0
|
15.5
|
0.5
|
|
C1D
|
J:HEM200
|
3.0
|
8.2
|
0.5
|
|
C1A
|
I:HEM200
|
3.0
|
13.1
|
0.5
|
|
C1B
|
J:HEM200
|
3.0
|
6.2
|
0.5
|
|
C1A
|
J:HEM200
|
3.0
|
6.1
|
0.5
|
|
C4D
|
J:HEM200
|
3.0
|
7.7
|
0.5
|
|
C4A
|
J:HEM200
|
3.0
|
5.5
|
0.5
|
|
C1C
|
J:HEM200
|
3.1
|
8.8
|
0.5
|
|
C4C
|
I:HEM200
|
3.1
|
16.0
|
0.5
|
|
C1C
|
I:HEM200
|
3.1
|
14.5
|
0.5
|
|
C4B
|
J:HEM200
|
3.1
|
6.8
|
0.5
|
|
C4A
|
I:HEM200
|
3.1
|
12.1
|
0.5
|
|
C1B
|
I:HEM200
|
3.1
|
12.8
|
0.5
|
|
C4B
|
I:HEM200
|
3.1
|
13.6
|
0.5
|
|
CE
|
I:MET52
|
3.2
|
9.5
|
1.0
|
|
CE
|
J:MET52
|
3.3
|
10.6
|
1.0
|
|
CHA
|
I:HEM200
|
3.4
|
14.0
|
0.5
|
|
CHD
|
J:HEM200
|
3.4
|
9.0
|
0.5
|
|
CG
|
I:MET52
|
3.4
|
7.0
|
1.0
|
|
CHD
|
I:HEM200
|
3.4
|
15.6
|
0.5
|
|
CHA
|
J:HEM200
|
3.4
|
7.2
|
0.5
|
|
CHB
|
J:HEM200
|
3.4
|
5.9
|
0.5
|
|
CHC
|
I:HEM200
|
3.5
|
13.7
|
0.5
|
|
CHC
|
J:HEM200
|
3.5
|
8.4
|
0.5
|
|
CHB
|
I:HEM200
|
3.5
|
12.5
|
0.5
|
|
CG
|
J:MET52
|
3.6
|
6.9
|
1.0
|
|
CB
|
I:MET52
|
4.1
|
7.4
|
1.0
|
|
C3D
|
I:HEM200
|
4.2
|
15.7
|
0.5
|
|
C2D
|
I:HEM200
|
4.2
|
15.8
|
0.5
|
|
C3C
|
J:HEM200
|
4.2
|
12.0
|
0.5
|
|
C2D
|
J:HEM200
|
4.2
|
9.1
|
0.5
|
|
C2A
|
I:HEM200
|
4.3
|
12.6
|
0.5
|
|
C3A
|
J:HEM200
|
4.3
|
5.9
|
0.5
|
|
C2C
|
J:HEM200
|
4.3
|
10.5
|
0.5
|
|
C3D
|
J:HEM200
|
4.3
|
9.4
|
0.5
|
|
C2A
|
J:HEM200
|
4.3
|
7.0
|
0.5
|
|
C2B
|
J:HEM200
|
4.3
|
7.2
|
0.5
|
|
C3A
|
I:HEM200
|
4.3
|
11.5
|
0.5
|
|
C3C
|
I:HEM200
|
4.3
|
16.4
|
0.5
|
|
C3B
|
J:HEM200
|
4.3
|
8.0
|
0.5
|
|
C2C
|
I:HEM200
|
4.3
|
14.2
|
0.5
|
|
CB
|
J:MET52
|
4.3
|
7.1
|
1.0
|
|
C2B
|
I:HEM200
|
4.3
|
12.4
|
0.5
|
|
C3B
|
I:HEM200
|
4.3
|
13.0
|
0.5
|
|
Reference:
S.V.Antonyuk,
M.A.Hough.
Monitoring and Validating Active Site Redox States in Protein Crystals. Biochim.Biophys.Acta V.1814 778 2011.
ISSN: ISSN 0006-3002
PubMed: 21215826
DOI: 10.1016/J.BBAPAP.2010.12.017
Page generated: Sun Aug 4 05:05:26 2024
|
