Iron in PDB 2vxi: The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
Protein crystallography data
The structure of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin, PDB code: 2vxi
was solved by
S.C.Willies,
M.N.Isupov,
E.F.Garman,
J.A.Littlechild,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
147.44 /
1.91
|
|
Space group
|
P 42 21 2
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
208.100,
208.100,
142.768,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
17.851 /
21.561
|
Other elements in 2vxi:
The structure of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin also contains other interesting chemical elements:
Iron Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Iron atom in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
(pdb code 2vxi). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 12 binding sites of Iron where determined in the
The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin, PDB code: 2vxi:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 12 in 2vxi
Go back to
Iron Binding Sites List in 2vxi
Iron binding site 1 out
of 12 in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe200
b:21.5
occ:0.50
|
FE
|
A:HEM200
|
0.0
|
21.5
|
0.5
|
|
FE
|
B:HEM200
|
0.0
|
22.3
|
0.5
|
|
NC
|
B:HEM200
|
1.9
|
17.4
|
0.5
|
|
NB
|
A:HEM200
|
2.0
|
6.7
|
0.5
|
|
NC
|
A:HEM200
|
2.0
|
12.2
|
0.5
|
|
NB
|
B:HEM200
|
2.0
|
13.1
|
0.5
|
|
NA
|
A:HEM200
|
2.0
|
11.2
|
0.5
|
|
ND
|
B:HEM200
|
2.1
|
13.4
|
0.5
|
|
NA
|
B:HEM200
|
2.1
|
13.5
|
0.5
|
|
ND
|
A:HEM200
|
2.1
|
13.9
|
0.5
|
|
SD
|
B:MET52
|
2.3
|
15.2
|
1.0
|
|
SD
|
A:MET52
|
2.4
|
15.5
|
1.0
|
|
C4C
|
B:HEM200
|
2.9
|
15.7
|
0.5
|
|
C4B
|
A:HEM200
|
2.9
|
7.4
|
0.5
|
|
C1B
|
A:HEM200
|
3.0
|
12.1
|
0.5
|
|
C1C
|
B:HEM200
|
3.0
|
15.2
|
0.5
|
|
C4A
|
A:HEM200
|
3.0
|
8.6
|
0.5
|
|
C4B
|
B:HEM200
|
3.0
|
14.7
|
0.5
|
|
C1D
|
B:HEM200
|
3.0
|
13.1
|
0.5
|
|
C1C
|
A:HEM200
|
3.0
|
14.2
|
0.5
|
|
C4C
|
A:HEM200
|
3.0
|
10.1
|
0.5
|
|
C1A
|
A:HEM200
|
3.0
|
12.8
|
0.5
|
|
C1A
|
B:HEM200
|
3.0
|
10.1
|
0.5
|
|
C1B
|
B:HEM200
|
3.0
|
13.3
|
0.5
|
|
C4D
|
B:HEM200
|
3.0
|
16.2
|
0.5
|
|
C4D
|
A:HEM200
|
3.1
|
14.6
|
0.5
|
|
C4A
|
B:HEM200
|
3.1
|
16.1
|
0.5
|
|
C1D
|
A:HEM200
|
3.1
|
16.7
|
0.5
|
|
CHD
|
B:HEM200
|
3.3
|
15.5
|
0.5
|
|
CHB
|
A:HEM200
|
3.3
|
8.1
|
0.5
|
|
CHC
|
A:HEM200
|
3.3
|
12.4
|
0.5
|
|
CHC
|
B:HEM200
|
3.3
|
16.6
|
0.5
|
|
CHA
|
A:HEM200
|
3.4
|
15.8
|
0.5
|
|
CHA
|
B:HEM200
|
3.4
|
12.0
|
0.5
|
|
CE
|
B:MET52
|
3.4
|
14.6
|
1.0
|
|
CHD
|
A:HEM200
|
3.4
|
13.8
|
0.5
|
|
CHB
|
B:HEM200
|
3.4
|
11.2
|
0.5
|
|
CG
|
B:MET52
|
3.4
|
12.1
|
1.0
|
|
CG
|
A:MET52
|
3.4
|
12.3
|
1.0
|
|
CE
|
A:MET52
|
3.6
|
17.1
|
1.0
|
|
C3C
|
B:HEM200
|
4.1
|
17.8
|
0.5
|
|
C3B
|
A:HEM200
|
4.1
|
10.6
|
0.5
|
|
CB
|
A:MET52
|
4.1
|
15.8
|
1.0
|
|
C2C
|
B:HEM200
|
4.1
|
13.8
|
0.5
|
|
CB
|
B:MET52
|
4.2
|
13.1
|
1.0
|
|
C2B
|
A:HEM200
|
4.2
|
2.2
|
0.5
|
|
C3C
|
A:HEM200
|
4.2
|
20.9
|
0.5
|
|
C3B
|
B:HEM200
|
4.2
|
21.7
|
0.5
|
|
C3A
|
A:HEM200
|
4.2
|
6.6
|
0.5
|
|
C2C
|
A:HEM200
|
4.2
|
15.6
|
0.5
|
|
C2B
|
B:HEM200
|
4.2
|
13.3
|
0.5
|
|
C2A
|
A:HEM200
|
4.2
|
15.8
|
0.5
|
|
C2D
|
B:HEM200
|
4.3
|
15.1
|
0.5
|
|
C3D
|
B:HEM200
|
4.3
|
12.9
|
0.5
|
|
C2A
|
B:HEM200
|
4.3
|
15.9
|
0.5
|
|
C3A
|
B:HEM200
|
4.3
|
9.8
|
0.5
|
|
C3D
|
A:HEM200
|
4.3
|
18.3
|
0.5
|
|
C2D
|
A:HEM200
|
4.3
|
15.2
|
0.5
|
|
Iron binding site 2 out
of 12 in 2vxi
Go back to
Iron Binding Sites List in 2vxi
Iron binding site 2 out
of 12 in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe200
b:22.3
occ:0.50
|
FE
|
A:HEM200
|
0.0
|
21.5
|
0.5
|
|
FE
|
B:HEM200
|
0.0
|
22.3
|
0.5
|
|
NC
|
B:HEM200
|
1.9
|
17.4
|
0.5
|
|
NB
|
A:HEM200
|
2.0
|
6.7
|
0.5
|
|
NC
|
A:HEM200
|
2.0
|
12.2
|
0.5
|
|
NB
|
B:HEM200
|
2.0
|
13.1
|
0.5
|
|
NA
|
A:HEM200
|
2.0
|
11.2
|
0.5
|
|
ND
|
B:HEM200
|
2.1
|
13.4
|
0.5
|
|
NA
|
B:HEM200
|
2.1
|
13.5
|
0.5
|
|
ND
|
A:HEM200
|
2.1
|
13.9
|
0.5
|
|
SD
|
B:MET52
|
2.3
|
15.2
|
1.0
|
|
SD
|
A:MET52
|
2.4
|
15.5
|
1.0
|
|
C4C
|
B:HEM200
|
2.9
|
15.7
|
0.5
|
|
C4B
|
A:HEM200
|
2.9
|
7.4
|
0.5
|
|
C1B
|
A:HEM200
|
3.0
|
12.1
|
0.5
|
|
C1C
|
B:HEM200
|
3.0
|
15.2
|
0.5
|
|
C4A
|
A:HEM200
|
3.0
|
8.6
|
0.5
|
|
C4B
|
B:HEM200
|
3.0
|
14.7
|
0.5
|
|
C1D
|
B:HEM200
|
3.0
|
13.1
|
0.5
|
|
C1C
|
A:HEM200
|
3.0
|
14.2
|
0.5
|
|
C4C
|
A:HEM200
|
3.0
|
10.1
|
0.5
|
|
C1A
|
A:HEM200
|
3.0
|
12.8
|
0.5
|
|
C1A
|
B:HEM200
|
3.0
|
10.1
|
0.5
|
|
C1B
|
B:HEM200
|
3.0
|
13.3
|
0.5
|
|
C4D
|
B:HEM200
|
3.0
|
16.2
|
0.5
|
|
C4D
|
A:HEM200
|
3.1
|
14.6
|
0.5
|
|
C4A
|
B:HEM200
|
3.1
|
16.1
|
0.5
|
|
C1D
|
A:HEM200
|
3.1
|
16.7
|
0.5
|
|
CHD
|
B:HEM200
|
3.3
|
15.5
|
0.5
|
|
CHB
|
A:HEM200
|
3.3
|
8.1
|
0.5
|
|
CHC
|
A:HEM200
|
3.3
|
12.4
|
0.5
|
|
CHC
|
B:HEM200
|
3.3
|
16.6
|
0.5
|
|
CHA
|
A:HEM200
|
3.4
|
15.8
|
0.5
|
|
CHA
|
B:HEM200
|
3.4
|
12.0
|
0.5
|
|
CE
|
B:MET52
|
3.4
|
14.6
|
1.0
|
|
CHD
|
A:HEM200
|
3.4
|
13.8
|
0.5
|
|
CHB
|
B:HEM200
|
3.4
|
11.2
|
0.5
|
|
CG
|
B:MET52
|
3.4
|
12.1
|
1.0
|
|
CG
|
A:MET52
|
3.4
|
12.3
|
1.0
|
|
CE
|
A:MET52
|
3.6
|
17.1
|
1.0
|
|
C3C
|
B:HEM200
|
4.1
|
17.8
|
0.5
|
|
C3B
|
A:HEM200
|
4.1
|
10.6
|
0.5
|
|
CB
|
A:MET52
|
4.1
|
15.8
|
1.0
|
|
C2C
|
B:HEM200
|
4.1
|
13.8
|
0.5
|
|
CB
|
B:MET52
|
4.2
|
13.1
|
1.0
|
|
C2B
|
A:HEM200
|
4.2
|
2.2
|
0.5
|
|
C3C
|
A:HEM200
|
4.2
|
20.9
|
0.5
|
|
C3B
|
B:HEM200
|
4.2
|
21.7
|
0.5
|
|
C3A
|
A:HEM200
|
4.2
|
6.6
|
0.5
|
|
C2C
|
A:HEM200
|
4.2
|
15.6
|
0.5
|
|
C2B
|
B:HEM200
|
4.2
|
13.3
|
0.5
|
|
C2A
|
A:HEM200
|
4.2
|
15.8
|
0.5
|
|
C2D
|
B:HEM200
|
4.3
|
15.1
|
0.5
|
|
C3D
|
B:HEM200
|
4.3
|
12.9
|
0.5
|
|
C2A
|
B:HEM200
|
4.3
|
15.9
|
0.5
|
|
C3A
|
B:HEM200
|
4.3
|
9.8
|
0.5
|
|
C3D
|
A:HEM200
|
4.3
|
18.3
|
0.5
|
|
C2D
|
A:HEM200
|
4.3
|
15.2
|
0.5
|
|
Iron binding site 3 out
of 12 in 2vxi
Go back to
Iron Binding Sites List in 2vxi
Iron binding site 3 out
of 12 in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe200
b:19.6
occ:0.50
|
FE
|
C:HEM200
|
0.0
|
19.6
|
0.5
|
|
FE
|
D:HEM200
|
0.0
|
21.5
|
0.5
|
|
NB
|
D:HEM200
|
2.0
|
14.4
|
0.5
|
|
NC
|
C:HEM200
|
2.0
|
8.0
|
0.5
|
|
NC
|
D:HEM200
|
2.0
|
14.4
|
0.5
|
|
NB
|
C:HEM200
|
2.0
|
11.6
|
0.5
|
|
NA
|
C:HEM200
|
2.0
|
12.7
|
0.5
|
|
ND
|
D:HEM200
|
2.1
|
19.2
|
0.5
|
|
NA
|
D:HEM200
|
2.1
|
12.8
|
0.5
|
|
ND
|
C:HEM200
|
2.2
|
9.3
|
0.5
|
|
SD
|
C:MET52
|
2.4
|
13.9
|
1.0
|
|
SD
|
D:MET52
|
2.4
|
14.9
|
1.0
|
|
C4B
|
D:HEM200
|
2.9
|
19.1
|
0.5
|
|
C4C
|
D:HEM200
|
3.0
|
13.5
|
0.5
|
|
C1C
|
D:HEM200
|
3.0
|
15.7
|
0.5
|
|
C4C
|
C:HEM200
|
3.0
|
11.6
|
0.5
|
|
C1C
|
C:HEM200
|
3.0
|
15.3
|
0.5
|
|
C1B
|
D:HEM200
|
3.0
|
14.2
|
0.5
|
|
C4A
|
C:HEM200
|
3.0
|
10.9
|
0.5
|
|
C1D
|
D:HEM200
|
3.0
|
15.1
|
0.5
|
|
C4B
|
C:HEM200
|
3.0
|
11.9
|
0.5
|
|
C1A
|
C:HEM200
|
3.0
|
13.2
|
0.5
|
|
C1B
|
C:HEM200
|
3.0
|
11.6
|
0.5
|
|
C4D
|
D:HEM200
|
3.0
|
16.1
|
0.5
|
|
C1A
|
D:HEM200
|
3.1
|
15.0
|
0.5
|
|
C4D
|
C:HEM200
|
3.1
|
10.4
|
0.5
|
|
C4A
|
D:HEM200
|
3.1
|
17.4
|
0.5
|
|
C1D
|
C:HEM200
|
3.1
|
15.6
|
0.5
|
|
CHD
|
D:HEM200
|
3.3
|
18.3
|
0.5
|
|
CHC
|
D:HEM200
|
3.3
|
17.4
|
0.5
|
|
CHB
|
C:HEM200
|
3.3
|
10.5
|
0.5
|
|
CE
|
C:MET52
|
3.4
|
9.2
|
1.0
|
|
CHA
|
C:HEM200
|
3.4
|
11.5
|
0.5
|
|
CHA
|
D:HEM200
|
3.4
|
17.9
|
0.5
|
|
CHC
|
C:HEM200
|
3.4
|
15.8
|
0.5
|
|
CHD
|
C:HEM200
|
3.4
|
9.5
|
0.5
|
|
CHB
|
D:HEM200
|
3.4
|
15.6
|
0.5
|
|
CE
|
D:MET52
|
3.4
|
12.4
|
1.0
|
|
CG
|
D:MET52
|
3.4
|
13.9
|
1.0
|
|
CG
|
C:MET52
|
3.5
|
11.7
|
1.0
|
|
CB
|
D:MET52
|
4.1
|
11.6
|
1.0
|
|
C3B
|
D:HEM200
|
4.1
|
20.1
|
0.5
|
|
C3C
|
D:HEM200
|
4.2
|
15.8
|
0.5
|
|
C3C
|
C:HEM200
|
4.2
|
17.0
|
0.5
|
|
C2B
|
D:HEM200
|
4.2
|
15.3
|
0.5
|
|
C2C
|
D:HEM200
|
4.2
|
11.7
|
0.5
|
|
CB
|
C:MET52
|
4.2
|
17.3
|
1.0
|
|
C3A
|
C:HEM200
|
4.2
|
10.2
|
0.5
|
|
C2C
|
C:HEM200
|
4.2
|
12.1
|
0.5
|
|
C2D
|
D:HEM200
|
4.2
|
16.8
|
0.5
|
|
C2A
|
C:HEM200
|
4.2
|
15.8
|
0.5
|
|
C3B
|
C:HEM200
|
4.2
|
9.9
|
0.5
|
|
C3D
|
D:HEM200
|
4.3
|
19.5
|
0.5
|
|
C2B
|
C:HEM200
|
4.3
|
9.9
|
0.5
|
|
C2A
|
D:HEM200
|
4.3
|
19.7
|
0.5
|
|
C3A
|
D:HEM200
|
4.3
|
16.9
|
0.5
|
|
C3D
|
C:HEM200
|
4.3
|
13.8
|
0.5
|
|
C2D
|
C:HEM200
|
4.4
|
16.6
|
0.5
|
|
Iron binding site 4 out
of 12 in 2vxi
Go back to
Iron Binding Sites List in 2vxi
Iron binding site 4 out
of 12 in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe200
b:21.5
occ:0.50
|
FE
|
D:HEM200
|
0.0
|
21.5
|
0.5
|
|
FE
|
C:HEM200
|
0.0
|
19.6
|
0.5
|
|
NB
|
D:HEM200
|
2.0
|
14.4
|
0.5
|
|
NC
|
C:HEM200
|
2.0
|
8.0
|
0.5
|
|
NC
|
D:HEM200
|
2.0
|
14.4
|
0.5
|
|
NB
|
C:HEM200
|
2.0
|
11.6
|
0.5
|
|
NA
|
C:HEM200
|
2.0
|
12.7
|
0.5
|
|
ND
|
D:HEM200
|
2.1
|
19.2
|
0.5
|
|
NA
|
D:HEM200
|
2.1
|
12.8
|
0.5
|
|
ND
|
C:HEM200
|
2.2
|
9.3
|
0.5
|
|
SD
|
C:MET52
|
2.4
|
13.9
|
1.0
|
|
SD
|
D:MET52
|
2.4
|
14.9
|
1.0
|
|
C4B
|
D:HEM200
|
2.9
|
19.1
|
0.5
|
|
C4C
|
D:HEM200
|
3.0
|
13.5
|
0.5
|
|
C1C
|
D:HEM200
|
3.0
|
15.7
|
0.5
|
|
C4C
|
C:HEM200
|
3.0
|
11.6
|
0.5
|
|
C4A
|
C:HEM200
|
3.0
|
10.9
|
0.5
|
|
C1C
|
C:HEM200
|
3.0
|
15.3
|
0.5
|
|
C1D
|
D:HEM200
|
3.0
|
15.1
|
0.5
|
|
C1B
|
D:HEM200
|
3.0
|
14.2
|
0.5
|
|
C4B
|
C:HEM200
|
3.0
|
11.9
|
0.5
|
|
C1A
|
C:HEM200
|
3.0
|
13.2
|
0.5
|
|
C1B
|
C:HEM200
|
3.0
|
11.6
|
0.5
|
|
C4D
|
D:HEM200
|
3.0
|
16.1
|
0.5
|
|
C1A
|
D:HEM200
|
3.1
|
15.0
|
0.5
|
|
C4D
|
C:HEM200
|
3.1
|
10.4
|
0.5
|
|
C4A
|
D:HEM200
|
3.1
|
17.4
|
0.5
|
|
C1D
|
C:HEM200
|
3.1
|
15.6
|
0.5
|
|
CHD
|
D:HEM200
|
3.3
|
18.3
|
0.5
|
|
CHC
|
D:HEM200
|
3.3
|
17.4
|
0.5
|
|
CHB
|
C:HEM200
|
3.3
|
10.5
|
0.5
|
|
CE
|
C:MET52
|
3.4
|
9.2
|
1.0
|
|
CHA
|
C:HEM200
|
3.4
|
11.5
|
0.5
|
|
CHA
|
D:HEM200
|
3.4
|
17.9
|
0.5
|
|
CHC
|
C:HEM200
|
3.4
|
15.8
|
0.5
|
|
CHD
|
C:HEM200
|
3.4
|
9.5
|
0.5
|
|
CHB
|
D:HEM200
|
3.4
|
15.6
|
0.5
|
|
CE
|
D:MET52
|
3.4
|
12.4
|
1.0
|
|
CG
|
D:MET52
|
3.4
|
13.9
|
1.0
|
|
CG
|
C:MET52
|
3.5
|
11.7
|
1.0
|
|
CB
|
D:MET52
|
4.1
|
11.6
|
1.0
|
|
C3B
|
D:HEM200
|
4.1
|
20.1
|
0.5
|
|
C3C
|
D:HEM200
|
4.2
|
15.8
|
0.5
|
|
C3C
|
C:HEM200
|
4.2
|
17.0
|
0.5
|
|
C2B
|
D:HEM200
|
4.2
|
15.3
|
0.5
|
|
C3A
|
C:HEM200
|
4.2
|
10.2
|
0.5
|
|
CB
|
C:MET52
|
4.2
|
17.3
|
1.0
|
|
C2C
|
D:HEM200
|
4.2
|
11.7
|
0.5
|
|
C2C
|
C:HEM200
|
4.2
|
12.1
|
0.5
|
|
C2D
|
D:HEM200
|
4.2
|
16.8
|
0.5
|
|
C2A
|
C:HEM200
|
4.2
|
15.8
|
0.5
|
|
C3B
|
C:HEM200
|
4.2
|
9.9
|
0.5
|
|
C3D
|
D:HEM200
|
4.3
|
19.5
|
0.5
|
|
C2B
|
C:HEM200
|
4.3
|
9.9
|
0.5
|
|
C2A
|
D:HEM200
|
4.3
|
19.7
|
0.5
|
|
C3D
|
C:HEM200
|
4.3
|
13.8
|
0.5
|
|
C3A
|
D:HEM200
|
4.3
|
16.9
|
0.5
|
|
C2D
|
C:HEM200
|
4.4
|
16.6
|
0.5
|
|
Iron binding site 5 out
of 12 in 2vxi
Go back to
Iron Binding Sites List in 2vxi
Iron binding site 5 out
of 12 in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe200
b:21.5
occ:0.50
|
FE
|
E:HEM200
|
0.0
|
21.5
|
0.5
|
|
FE
|
F:HEM200
|
0.0
|
22.2
|
0.5
|
|
NC
|
E:HEM200
|
2.0
|
13.2
|
0.5
|
|
NB
|
F:HEM200
|
2.0
|
15.7
|
0.5
|
|
NC
|
F:HEM200
|
2.1
|
13.7
|
0.5
|
|
NB
|
E:HEM200
|
2.1
|
11.9
|
0.5
|
|
NA
|
F:HEM200
|
2.1
|
14.1
|
0.5
|
|
ND
|
E:HEM200
|
2.1
|
17.1
|
0.5
|
|
NA
|
E:HEM200
|
2.1
|
13.8
|
0.5
|
|
ND
|
F:HEM200
|
2.2
|
14.2
|
0.5
|
|
SD
|
F:MET52
|
2.3
|
14.5
|
1.0
|
|
SD
|
E:MET52
|
2.4
|
14.1
|
1.0
|
|
C4C
|
E:HEM200
|
2.9
|
6.3
|
0.5
|
|
C1B
|
F:HEM200
|
3.0
|
14.1
|
0.5
|
|
C4B
|
F:HEM200
|
3.0
|
13.2
|
0.5
|
|
C1C
|
E:HEM200
|
3.0
|
8.6
|
0.5
|
|
C4A
|
F:HEM200
|
3.0
|
15.6
|
0.5
|
|
C4C
|
F:HEM200
|
3.0
|
10.1
|
0.5
|
|
C1D
|
E:HEM200
|
3.0
|
16.3
|
0.5
|
|
C4B
|
E:HEM200
|
3.0
|
8.8
|
0.5
|
|
C1B
|
E:HEM200
|
3.0
|
12.7
|
0.5
|
|
C1C
|
F:HEM200
|
3.1
|
11.1
|
0.5
|
|
C4A
|
E:HEM200
|
3.1
|
15.8
|
0.5
|
|
C1D
|
F:HEM200
|
3.1
|
12.3
|
0.5
|
|
C1A
|
F:HEM200
|
3.1
|
18.7
|
0.5
|
|
C4D
|
E:HEM200
|
3.1
|
11.6
|
0.5
|
|
C1A
|
E:HEM200
|
3.1
|
13.6
|
0.5
|
|
C4D
|
F:HEM200
|
3.1
|
15.6
|
0.5
|
|
CHD
|
E:HEM200
|
3.3
|
14.9
|
0.5
|
|
CHB
|
F:HEM200
|
3.3
|
11.8
|
0.5
|
|
CHC
|
E:HEM200
|
3.3
|
7.7
|
0.5
|
|
CHD
|
F:HEM200
|
3.3
|
9.9
|
0.5
|
|
CE
|
F:MET52
|
3.4
|
14.7
|
1.0
|
|
CHC
|
F:HEM200
|
3.4
|
17.5
|
0.5
|
|
CHB
|
E:HEM200
|
3.4
|
12.7
|
0.5
|
|
CE
|
E:MET52
|
3.4
|
12.2
|
1.0
|
|
CG
|
E:MET52
|
3.4
|
12.1
|
1.0
|
|
CHA
|
E:HEM200
|
3.5
|
14.5
|
0.5
|
|
CHA
|
F:HEM200
|
3.5
|
17.0
|
0.5
|
|
CG
|
F:MET52
|
3.5
|
12.4
|
1.0
|
|
CB
|
E:MET52
|
4.1
|
15.6
|
1.0
|
|
C3C
|
E:HEM200
|
4.1
|
14.0
|
0.5
|
|
C3B
|
F:HEM200
|
4.2
|
14.2
|
0.5
|
|
C2B
|
F:HEM200
|
4.2
|
17.0
|
0.5
|
|
C2C
|
E:HEM200
|
4.2
|
7.0
|
0.5
|
|
CB
|
F:MET52
|
4.2
|
15.7
|
1.0
|
|
C3C
|
F:HEM200
|
4.2
|
14.5
|
0.5
|
|
C3A
|
F:HEM200
|
4.2
|
15.5
|
0.5
|
|
C3B
|
E:HEM200
|
4.2
|
8.6
|
0.5
|
|
C2D
|
E:HEM200
|
4.3
|
18.5
|
0.5
|
|
C2B
|
E:HEM200
|
4.3
|
16.3
|
0.5
|
|
C2C
|
F:HEM200
|
4.3
|
16.9
|
0.5
|
|
C2A
|
F:HEM200
|
4.3
|
19.6
|
0.5
|
|
C3A
|
E:HEM200
|
4.3
|
13.6
|
0.5
|
|
C3D
|
E:HEM200
|
4.3
|
16.0
|
0.5
|
|
C2A
|
E:HEM200
|
4.3
|
11.6
|
0.5
|
|
C2D
|
F:HEM200
|
4.3
|
18.4
|
0.5
|
|
C3D
|
F:HEM200
|
4.4
|
15.2
|
0.5
|
|
Iron binding site 6 out
of 12 in 2vxi
Go back to
Iron Binding Sites List in 2vxi
Iron binding site 6 out
of 12 in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe200
b:22.2
occ:0.50
|
FE
|
F:HEM200
|
0.0
|
22.2
|
0.5
|
|
FE
|
E:HEM200
|
0.0
|
21.5
|
0.5
|
|
NC
|
E:HEM200
|
2.0
|
13.2
|
0.5
|
|
NB
|
F:HEM200
|
2.0
|
15.7
|
0.5
|
|
NC
|
F:HEM200
|
2.1
|
13.7
|
0.5
|
|
NB
|
E:HEM200
|
2.1
|
11.9
|
0.5
|
|
NA
|
F:HEM200
|
2.1
|
14.1
|
0.5
|
|
ND
|
E:HEM200
|
2.1
|
17.1
|
0.5
|
|
NA
|
E:HEM200
|
2.1
|
13.8
|
0.5
|
|
ND
|
F:HEM200
|
2.2
|
14.2
|
0.5
|
|
SD
|
F:MET52
|
2.3
|
14.5
|
1.0
|
|
SD
|
E:MET52
|
2.4
|
14.1
|
1.0
|
|
C4C
|
E:HEM200
|
2.9
|
6.3
|
0.5
|
|
C1B
|
F:HEM200
|
3.0
|
14.1
|
0.5
|
|
C4B
|
F:HEM200
|
3.0
|
13.2
|
0.5
|
|
C1C
|
E:HEM200
|
3.0
|
8.6
|
0.5
|
|
C4A
|
F:HEM200
|
3.0
|
15.6
|
0.5
|
|
C4C
|
F:HEM200
|
3.0
|
10.1
|
0.5
|
|
C1D
|
E:HEM200
|
3.0
|
16.3
|
0.5
|
|
C4B
|
E:HEM200
|
3.0
|
8.8
|
0.5
|
|
C1B
|
E:HEM200
|
3.0
|
12.7
|
0.5
|
|
C1C
|
F:HEM200
|
3.1
|
11.1
|
0.5
|
|
C4A
|
E:HEM200
|
3.1
|
15.8
|
0.5
|
|
C1D
|
F:HEM200
|
3.1
|
12.3
|
0.5
|
|
C1A
|
F:HEM200
|
3.1
|
18.7
|
0.5
|
|
C4D
|
E:HEM200
|
3.1
|
11.6
|
0.5
|
|
C1A
|
E:HEM200
|
3.1
|
13.6
|
0.5
|
|
C4D
|
F:HEM200
|
3.1
|
15.6
|
0.5
|
|
CHD
|
E:HEM200
|
3.3
|
14.9
|
0.5
|
|
CHB
|
F:HEM200
|
3.3
|
11.8
|
0.5
|
|
CHD
|
F:HEM200
|
3.3
|
9.9
|
0.5
|
|
CHC
|
E:HEM200
|
3.3
|
7.7
|
0.5
|
|
CE
|
F:MET52
|
3.4
|
14.7
|
1.0
|
|
CHC
|
F:HEM200
|
3.4
|
17.5
|
0.5
|
|
CHB
|
E:HEM200
|
3.4
|
12.7
|
0.5
|
|
CE
|
E:MET52
|
3.4
|
12.2
|
1.0
|
|
CG
|
E:MET52
|
3.4
|
12.1
|
1.0
|
|
CHA
|
E:HEM200
|
3.5
|
14.5
|
0.5
|
|
CHA
|
F:HEM200
|
3.5
|
17.0
|
0.5
|
|
CG
|
F:MET52
|
3.5
|
12.4
|
1.0
|
|
CB
|
E:MET52
|
4.1
|
15.6
|
1.0
|
|
C3C
|
E:HEM200
|
4.1
|
14.0
|
0.5
|
|
C3B
|
F:HEM200
|
4.2
|
14.2
|
0.5
|
|
C2B
|
F:HEM200
|
4.2
|
17.0
|
0.5
|
|
C2C
|
E:HEM200
|
4.2
|
7.0
|
0.5
|
|
CB
|
F:MET52
|
4.2
|
15.7
|
1.0
|
|
C3C
|
F:HEM200
|
4.2
|
14.5
|
0.5
|
|
C3A
|
F:HEM200
|
4.2
|
15.5
|
0.5
|
|
C3B
|
E:HEM200
|
4.2
|
8.6
|
0.5
|
|
C2D
|
E:HEM200
|
4.3
|
18.5
|
0.5
|
|
C2B
|
E:HEM200
|
4.3
|
16.3
|
0.5
|
|
C2C
|
F:HEM200
|
4.3
|
16.9
|
0.5
|
|
C2A
|
F:HEM200
|
4.3
|
19.6
|
0.5
|
|
C3A
|
E:HEM200
|
4.3
|
13.6
|
0.5
|
|
C3D
|
E:HEM200
|
4.3
|
16.0
|
0.5
|
|
C2A
|
E:HEM200
|
4.3
|
11.6
|
0.5
|
|
C2D
|
F:HEM200
|
4.3
|
18.4
|
0.5
|
|
C3D
|
F:HEM200
|
4.4
|
15.2
|
0.5
|
|
Iron binding site 7 out
of 12 in 2vxi
Go back to
Iron Binding Sites List in 2vxi
Iron binding site 7 out
of 12 in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Fe200
b:22.2
occ:0.50
|
FE
|
G:HEM200
|
0.0
|
22.2
|
0.5
|
|
FE
|
H:HEM200
|
0.0
|
20.6
|
0.5
|
|
NC
|
H:HEM200
|
2.0
|
12.2
|
0.5
|
|
NB
|
G:HEM200
|
2.0
|
15.7
|
0.5
|
|
NB
|
H:HEM200
|
2.0
|
12.1
|
0.5
|
|
NC
|
G:HEM200
|
2.0
|
13.6
|
0.5
|
|
NA
|
G:HEM200
|
2.1
|
13.7
|
0.5
|
|
ND
|
H:HEM200
|
2.1
|
11.9
|
0.5
|
|
NA
|
H:HEM200
|
2.2
|
13.0
|
0.5
|
|
ND
|
G:HEM200
|
2.2
|
16.7
|
0.5
|
|
SD
|
G:MET52
|
2.3
|
13.9
|
1.0
|
|
SD
|
H:MET52
|
2.4
|
15.7
|
1.0
|
|
C4C
|
H:HEM200
|
2.9
|
8.8
|
0.5
|
|
C1B
|
G:HEM200
|
2.9
|
18.0
|
0.5
|
|
C4B
|
G:HEM200
|
2.9
|
15.0
|
0.5
|
|
C1C
|
H:HEM200
|
3.0
|
7.6
|
0.5
|
|
C4B
|
H:HEM200
|
3.0
|
7.6
|
0.5
|
|
C4C
|
G:HEM200
|
3.0
|
15.5
|
0.5
|
|
C1C
|
G:HEM200
|
3.0
|
18.2
|
0.5
|
|
C1B
|
H:HEM200
|
3.0
|
10.6
|
0.5
|
|
C4A
|
G:HEM200
|
3.0
|
12.2
|
0.5
|
|
C1D
|
H:HEM200
|
3.1
|
12.3
|
0.5
|
|
C1A
|
G:HEM200
|
3.1
|
10.7
|
0.5
|
|
C4D
|
H:HEM200
|
3.1
|
11.2
|
0.5
|
|
C4A
|
H:HEM200
|
3.1
|
10.7
|
0.5
|
|
C1D
|
G:HEM200
|
3.1
|
13.7
|
0.5
|
|
C1A
|
H:HEM200
|
3.2
|
14.7
|
0.5
|
|
C4D
|
G:HEM200
|
3.2
|
15.6
|
0.5
|
|
CHD
|
H:HEM200
|
3.3
|
11.9
|
0.5
|
|
CE
|
G:MET52
|
3.3
|
10.8
|
1.0
|
|
CHB
|
G:HEM200
|
3.3
|
14.2
|
0.5
|
|
CHC
|
H:HEM200
|
3.3
|
13.0
|
0.5
|
|
CHC
|
G:HEM200
|
3.3
|
18.6
|
0.5
|
|
CHD
|
G:HEM200
|
3.4
|
16.8
|
0.5
|
|
CHB
|
H:HEM200
|
3.4
|
10.1
|
0.5
|
|
CG
|
H:MET52
|
3.4
|
12.8
|
1.0
|
|
CE
|
H:MET52
|
3.4
|
8.9
|
1.0
|
|
CG
|
G:MET52
|
3.4
|
13.9
|
1.0
|
|
CHA
|
H:HEM200
|
3.5
|
13.8
|
0.5
|
|
CHA
|
G:HEM200
|
3.5
|
15.0
|
0.5
|
|
C3C
|
H:HEM200
|
4.1
|
13.2
|
0.5
|
|
C3B
|
G:HEM200
|
4.1
|
17.5
|
0.5
|
|
CB
|
H:MET52
|
4.1
|
11.1
|
1.0
|
|
C2B
|
G:HEM200
|
4.1
|
16.4
|
0.5
|
|
C2C
|
H:HEM200
|
4.2
|
6.3
|
0.5
|
|
C3C
|
G:HEM200
|
4.2
|
19.0
|
0.5
|
|
C3B
|
H:HEM200
|
4.2
|
12.3
|
0.5
|
|
CB
|
G:MET52
|
4.2
|
14.6
|
1.0
|
|
C2B
|
H:HEM200
|
4.2
|
16.0
|
0.5
|
|
C2C
|
G:HEM200
|
4.3
|
18.3
|
0.5
|
|
C3A
|
G:HEM200
|
4.3
|
12.1
|
0.5
|
|
C2D
|
H:HEM200
|
4.3
|
6.8
|
0.5
|
|
C2A
|
G:HEM200
|
4.3
|
14.0
|
0.5
|
|
C3D
|
H:HEM200
|
4.3
|
12.4
|
0.5
|
|
C3A
|
H:HEM200
|
4.4
|
12.5
|
0.5
|
|
C2A
|
H:HEM200
|
4.4
|
11.6
|
0.5
|
|
C2D
|
G:HEM200
|
4.4
|
18.7
|
0.5
|
|
C3D
|
G:HEM200
|
4.4
|
13.9
|
0.5
|
|
Iron binding site 8 out
of 12 in 2vxi
Go back to
Iron Binding Sites List in 2vxi
Iron binding site 8 out
of 12 in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Fe200
b:20.6
occ:0.50
|
FE
|
H:HEM200
|
0.0
|
20.6
|
0.5
|
|
FE
|
G:HEM200
|
0.0
|
22.2
|
0.5
|
|
NC
|
H:HEM200
|
2.0
|
12.2
|
0.5
|
|
NB
|
G:HEM200
|
2.0
|
15.7
|
0.5
|
|
NB
|
H:HEM200
|
2.0
|
12.1
|
0.5
|
|
NC
|
G:HEM200
|
2.0
|
13.6
|
0.5
|
|
NA
|
G:HEM200
|
2.1
|
13.7
|
0.5
|
|
ND
|
H:HEM200
|
2.1
|
11.9
|
0.5
|
|
NA
|
H:HEM200
|
2.2
|
13.0
|
0.5
|
|
ND
|
G:HEM200
|
2.2
|
16.7
|
0.5
|
|
SD
|
G:MET52
|
2.3
|
13.9
|
1.0
|
|
SD
|
H:MET52
|
2.4
|
15.7
|
1.0
|
|
C4C
|
H:HEM200
|
2.9
|
8.8
|
0.5
|
|
C1B
|
G:HEM200
|
2.9
|
18.0
|
0.5
|
|
C4B
|
G:HEM200
|
3.0
|
15.0
|
0.5
|
|
C1C
|
H:HEM200
|
3.0
|
7.6
|
0.5
|
|
C4B
|
H:HEM200
|
3.0
|
7.6
|
0.5
|
|
C4C
|
G:HEM200
|
3.0
|
15.5
|
0.5
|
|
C1C
|
G:HEM200
|
3.0
|
18.2
|
0.5
|
|
C1B
|
H:HEM200
|
3.0
|
10.6
|
0.5
|
|
C4A
|
G:HEM200
|
3.0
|
12.2
|
0.5
|
|
C1D
|
H:HEM200
|
3.1
|
12.3
|
0.5
|
|
C1A
|
G:HEM200
|
3.1
|
10.7
|
0.5
|
|
C4D
|
H:HEM200
|
3.1
|
11.2
|
0.5
|
|
C4A
|
H:HEM200
|
3.1
|
10.7
|
0.5
|
|
C1D
|
G:HEM200
|
3.1
|
13.7
|
0.5
|
|
C1A
|
H:HEM200
|
3.2
|
14.7
|
0.5
|
|
C4D
|
G:HEM200
|
3.2
|
15.6
|
0.5
|
|
CHD
|
H:HEM200
|
3.3
|
11.9
|
0.5
|
|
CE
|
G:MET52
|
3.3
|
10.8
|
1.0
|
|
CHB
|
G:HEM200
|
3.3
|
14.2
|
0.5
|
|
CHC
|
H:HEM200
|
3.3
|
13.0
|
0.5
|
|
CHC
|
G:HEM200
|
3.3
|
18.6
|
0.5
|
|
CHD
|
G:HEM200
|
3.4
|
16.8
|
0.5
|
|
CHB
|
H:HEM200
|
3.4
|
10.1
|
0.5
|
|
CG
|
H:MET52
|
3.4
|
12.8
|
1.0
|
|
CE
|
H:MET52
|
3.4
|
8.9
|
1.0
|
|
CG
|
G:MET52
|
3.4
|
13.9
|
1.0
|
|
CHA
|
H:HEM200
|
3.5
|
13.8
|
0.5
|
|
CHA
|
G:HEM200
|
3.5
|
15.0
|
0.5
|
|
C3C
|
H:HEM200
|
4.1
|
13.2
|
0.5
|
|
C3B
|
G:HEM200
|
4.1
|
17.5
|
0.5
|
|
CB
|
H:MET52
|
4.1
|
11.1
|
1.0
|
|
C2B
|
G:HEM200
|
4.1
|
16.4
|
0.5
|
|
C2C
|
H:HEM200
|
4.2
|
6.3
|
0.5
|
|
C3C
|
G:HEM200
|
4.2
|
19.0
|
0.5
|
|
C3B
|
H:HEM200
|
4.2
|
12.3
|
0.5
|
|
CB
|
G:MET52
|
4.2
|
14.6
|
1.0
|
|
C2B
|
H:HEM200
|
4.2
|
16.0
|
0.5
|
|
C2C
|
G:HEM200
|
4.3
|
18.3
|
0.5
|
|
C3A
|
G:HEM200
|
4.3
|
12.1
|
0.5
|
|
C2D
|
H:HEM200
|
4.3
|
6.8
|
0.5
|
|
C2A
|
G:HEM200
|
4.3
|
14.0
|
0.5
|
|
C3D
|
H:HEM200
|
4.3
|
12.4
|
0.5
|
|
C3A
|
H:HEM200
|
4.4
|
12.5
|
0.5
|
|
C2A
|
H:HEM200
|
4.4
|
11.6
|
0.5
|
|
C2D
|
G:HEM200
|
4.4
|
18.7
|
0.5
|
|
C3D
|
G:HEM200
|
4.4
|
13.9
|
0.5
|
|
Iron binding site 9 out
of 12 in 2vxi
Go back to
Iron Binding Sites List in 2vxi
Iron binding site 9 out
of 12 in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Fe200
b:23.3
occ:0.50
|
FE
|
I:HEM200
|
0.0
|
23.3
|
0.5
|
|
FE
|
J:HEM200
|
0.0
|
21.2
|
0.5
|
|
NB
|
I:HEM200
|
1.9
|
16.4
|
0.5
|
|
NC
|
J:HEM200
|
2.0
|
6.4
|
0.5
|
|
NC
|
I:HEM200
|
2.0
|
17.5
|
0.5
|
|
NB
|
J:HEM200
|
2.0
|
9.4
|
0.5
|
|
NA
|
I:HEM200
|
2.1
|
15.6
|
0.5
|
|
NA
|
J:HEM200
|
2.1
|
12.5
|
0.5
|
|
ND
|
J:HEM200
|
2.1
|
14.4
|
0.5
|
|
ND
|
I:HEM200
|
2.1
|
16.0
|
0.5
|
|
SD
|
I:MET52
|
2.3
|
15.8
|
1.0
|
|
SD
|
J:MET52
|
2.4
|
14.8
|
1.0
|
|
C4C
|
J:HEM200
|
2.9
|
4.4
|
0.5
|
|
C1B
|
I:HEM200
|
2.9
|
17.9
|
0.5
|
|
C4B
|
I:HEM200
|
3.0
|
20.3
|
0.5
|
|
C4B
|
J:HEM200
|
3.0
|
13.0
|
0.5
|
|
C4C
|
I:HEM200
|
3.0
|
16.4
|
0.5
|
|
C1C
|
I:HEM200
|
3.0
|
20.3
|
0.5
|
|
C1C
|
J:HEM200
|
3.0
|
7.4
|
0.5
|
|
C4A
|
I:HEM200
|
3.0
|
16.7
|
0.5
|
|
C1D
|
J:HEM200
|
3.0
|
15.9
|
0.5
|
|
C1B
|
J:HEM200
|
3.0
|
10.0
|
0.5
|
|
C1A
|
J:HEM200
|
3.1
|
15.6
|
0.5
|
|
C4D
|
I:HEM200
|
3.1
|
16.6
|
0.5
|
|
C1A
|
I:HEM200
|
3.1
|
15.8
|
0.5
|
|
C4D
|
J:HEM200
|
3.1
|
16.8
|
0.5
|
|
C4A
|
J:HEM200
|
3.1
|
12.3
|
0.5
|
|
C1D
|
I:HEM200
|
3.1
|
15.4
|
0.5
|
|
CHD
|
J:HEM200
|
3.3
|
11.6
|
0.5
|
|
CHB
|
I:HEM200
|
3.3
|
10.6
|
0.5
|
|
CE
|
I:MET52
|
3.4
|
11.9
|
1.0
|
|
CHC
|
I:HEM200
|
3.4
|
18.3
|
0.5
|
|
CG
|
I:MET52
|
3.4
|
11.6
|
1.0
|
|
CHA
|
J:HEM200
|
3.4
|
14.9
|
0.5
|
|
CHA
|
I:HEM200
|
3.4
|
18.1
|
0.5
|
|
CHC
|
J:HEM200
|
3.4
|
10.0
|
0.5
|
|
CHD
|
I:HEM200
|
3.4
|
11.3
|
0.5
|
|
CHB
|
J:HEM200
|
3.4
|
13.8
|
0.5
|
|
CE
|
J:MET52
|
3.5
|
12.8
|
1.0
|
|
CG
|
J:MET52
|
3.5
|
11.1
|
1.0
|
|
C3C
|
J:HEM200
|
4.1
|
12.9
|
0.5
|
|
CB
|
I:MET52
|
4.1
|
10.3
|
1.0
|
|
C2B
|
I:HEM200
|
4.2
|
14.8
|
0.5
|
|
C3B
|
I:HEM200
|
4.2
|
17.9
|
0.5
|
|
C2C
|
J:HEM200
|
4.2
|
5.8
|
0.5
|
|
C3C
|
I:HEM200
|
4.2
|
14.8
|
0.5
|
|
C3B
|
J:HEM200
|
4.2
|
11.8
|
0.5
|
|
C2C
|
I:HEM200
|
4.2
|
17.5
|
0.5
|
|
CB
|
J:MET52
|
4.2
|
12.5
|
1.0
|
|
C2B
|
J:HEM200
|
4.3
|
11.3
|
0.5
|
|
C3A
|
I:HEM200
|
4.3
|
9.2
|
0.5
|
|
C2A
|
I:HEM200
|
4.3
|
19.6
|
0.5
|
|
C2D
|
J:HEM200
|
4.3
|
16.6
|
0.5
|
|
C2A
|
J:HEM200
|
4.3
|
14.3
|
0.5
|
|
C3D
|
J:HEM200
|
4.3
|
19.1
|
0.5
|
|
C3A
|
J:HEM200
|
4.3
|
14.3
|
0.5
|
|
C3D
|
I:HEM200
|
4.3
|
15.6
|
0.5
|
|
C2D
|
I:HEM200
|
4.3
|
15.4
|
0.5
|
|
Iron binding site 10 out
of 12 in 2vxi
Go back to
Iron Binding Sites List in 2vxi
Iron binding site 10 out
of 12 in the The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of The Binding of Heme and Zinc in Escherichia Coli Bacterioferritin within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Fe200
b:21.2
occ:0.50
|
FE
|
J:HEM200
|
0.0
|
21.2
|
0.5
|
|
FE
|
I:HEM200
|
0.0
|
23.3
|
0.5
|
|
NB
|
I:HEM200
|
1.9
|
16.4
|
0.5
|
|
NC
|
J:HEM200
|
2.0
|
6.4
|
0.5
|
|
NC
|
I:HEM200
|
2.0
|
17.5
|
0.5
|
|
NB
|
J:HEM200
|
2.0
|
9.4
|
0.5
|
|
NA
|
I:HEM200
|
2.1
|
15.6
|
0.5
|
|
NA
|
J:HEM200
|
2.1
|
12.5
|
0.5
|
|
ND
|
J:HEM200
|
2.1
|
14.4
|
0.5
|
|
ND
|
I:HEM200
|
2.1
|
16.0
|
0.5
|
|
SD
|
I:MET52
|
2.3
|
15.8
|
1.0
|
|
SD
|
J:MET52
|
2.4
|
14.8
|
1.0
|
|
C4C
|
J:HEM200
|
2.9
|
4.4
|
0.5
|
|
C1B
|
I:HEM200
|
2.9
|
17.9
|
0.5
|
|
C4B
|
I:HEM200
|
3.0
|
20.3
|
0.5
|
|
C4B
|
J:HEM200
|
3.0
|
13.0
|
0.5
|
|
C4C
|
I:HEM200
|
3.0
|
16.4
|
0.5
|
|
C1C
|
I:HEM200
|
3.0
|
20.3
|
0.5
|
|
C1C
|
J:HEM200
|
3.0
|
7.4
|
0.5
|
|
C4A
|
I:HEM200
|
3.0
|
16.7
|
0.5
|
|
C1D
|
J:HEM200
|
3.0
|
15.9
|
0.5
|
|
C1B
|
J:HEM200
|
3.0
|
10.0
|
0.5
|
|
C1A
|
J:HEM200
|
3.1
|
15.6
|
0.5
|
|
C1A
|
I:HEM200
|
3.1
|
15.8
|
0.5
|
|
C4D
|
I:HEM200
|
3.1
|
16.6
|
0.5
|
|
C4D
|
J:HEM200
|
3.1
|
16.8
|
0.5
|
|
C4A
|
J:HEM200
|
3.1
|
12.3
|
0.5
|
|
C1D
|
I:HEM200
|
3.1
|
15.4
|
0.5
|
|
CHD
|
J:HEM200
|
3.3
|
11.6
|
0.5
|
|
CHB
|
I:HEM200
|
3.3
|
10.6
|
0.5
|
|
CE
|
I:MET52
|
3.4
|
11.9
|
1.0
|
|
CHC
|
I:HEM200
|
3.4
|
18.3
|
0.5
|
|
CG
|
I:MET52
|
3.4
|
11.6
|
1.0
|
|
CHA
|
J:HEM200
|
3.4
|
14.9
|
0.5
|
|
CHA
|
I:HEM200
|
3.4
|
18.1
|
0.5
|
|
CHC
|
J:HEM200
|
3.4
|
10.0
|
0.5
|
|
CHD
|
I:HEM200
|
3.4
|
11.3
|
0.5
|
|
CHB
|
J:HEM200
|
3.4
|
13.8
|
0.5
|
|
CE
|
J:MET52
|
3.5
|
12.8
|
1.0
|
|
CG
|
J:MET52
|
3.5
|
11.1
|
1.0
|
|
C3C
|
J:HEM200
|
4.1
|
12.9
|
0.5
|
|
CB
|
I:MET52
|
4.1
|
10.3
|
1.0
|
|
C2B
|
I:HEM200
|
4.1
|
14.8
|
0.5
|
|
C3B
|
I:HEM200
|
4.2
|
17.9
|
0.5
|
|
C2C
|
J:HEM200
|
4.2
|
5.8
|
0.5
|
|
C3C
|
I:HEM200
|
4.2
|
14.8
|
0.5
|
|
C3B
|
J:HEM200
|
4.2
|
11.8
|
0.5
|
|
C2C
|
I:HEM200
|
4.2
|
17.5
|
0.5
|
|
CB
|
J:MET52
|
4.2
|
12.5
|
1.0
|
|
C2B
|
J:HEM200
|
4.3
|
11.3
|
0.5
|
|
C3A
|
I:HEM200
|
4.3
|
9.2
|
0.5
|
|
C2A
|
I:HEM200
|
4.3
|
19.6
|
0.5
|
|
C2D
|
J:HEM200
|
4.3
|
16.6
|
0.5
|
|
C2A
|
J:HEM200
|
4.3
|
14.3
|
0.5
|
|
C3D
|
J:HEM200
|
4.3
|
19.1
|
0.5
|
|
C3A
|
J:HEM200
|
4.3
|
14.3
|
0.5
|
|
C3D
|
I:HEM200
|
4.3
|
15.6
|
0.5
|
|
C2D
|
I:HEM200
|
4.3
|
15.4
|
0.5
|
|
Reference:
S.C.Willies,
M.N.Isupov,
E.F.Garman,
J.A.Littlechild.
The Binding of Haem and Zinc in the 1.9 A X-Ray Structure of Escherichia Coli Bacterioferritin. J.Biol.Inorg.Chem. V. 14 201 2009.
ISSN: ISSN 0949-8257
PubMed: 18946693
DOI: 10.1007/S00775-008-0438-8
Page generated: Sun Aug 4 03:11:27 2024
|
