Iron in PDB 3uoi: Mycobacterium Tuberculosis Bacterioferritin, Bfra
Enzymatic activity of Mycobacterium Tuberculosis Bacterioferritin, Bfra
All present enzymatic activity of Mycobacterium Tuberculosis Bacterioferritin, Bfra:
1.16.3.1;
Protein crystallography data
The structure of Mycobacterium Tuberculosis Bacterioferritin, Bfra, PDB code: 3uoi
was solved by
L.M.Mcmath,
C.W.Goulding,
Tb Structural Genomics Consortium (Tbsgc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
32.56 /
1.90
|
|
Space group
|
P 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
122.962,
123.225,
175.452,
89.95,
89.95,
90.00
|
|
R / Rfree (%)
|
14.8 /
19.4
|
Iron Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
24;
Binding sites:
The binding sites of Iron atom in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
(pdb code 3uoi). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 24 binding sites of Iron where determined in the
Mycobacterium Tuberculosis Bacterioferritin, Bfra, PDB code: 3uoi:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 24 in 3uoi
Go back to
Iron Binding Sites List in 3uoi
Iron binding site 1 out
of 24 in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Mycobacterium Tuberculosis Bacterioferritin, Bfra within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe200
b:23.1
occ:1.00
|
FE
|
B:HEM200
|
0.0
|
23.1
|
1.0
|
|
ND
|
B:HEM200
|
1.9
|
20.5
|
1.0
|
|
NC
|
B:HEM200
|
2.1
|
25.0
|
1.0
|
|
NB
|
B:HEM200
|
2.1
|
24.6
|
1.0
|
|
NA
|
B:HEM200
|
2.2
|
24.5
|
1.0
|
|
SD
|
B:MET52
|
2.2
|
16.1
|
1.0
|
|
SD
|
A:MET52
|
2.3
|
21.6
|
1.0
|
|
C4D
|
B:HEM200
|
2.9
|
27.9
|
1.0
|
|
C1D
|
B:HEM200
|
3.0
|
23.2
|
1.0
|
|
C4C
|
B:HEM200
|
3.1
|
21.1
|
1.0
|
|
C1C
|
B:HEM200
|
3.1
|
24.6
|
1.0
|
|
C1A
|
B:HEM200
|
3.1
|
26.8
|
1.0
|
|
C4B
|
B:HEM200
|
3.1
|
27.1
|
1.0
|
|
C4A
|
B:HEM200
|
3.2
|
25.0
|
1.0
|
|
C1B
|
B:HEM200
|
3.2
|
28.1
|
1.0
|
|
CE
|
B:MET52
|
3.2
|
19.8
|
1.0
|
|
CHA
|
B:HEM200
|
3.4
|
24.7
|
1.0
|
|
CHD
|
B:HEM200
|
3.4
|
19.2
|
1.0
|
|
CE
|
A:MET52
|
3.4
|
17.2
|
1.0
|
|
CHC
|
B:HEM200
|
3.4
|
25.0
|
1.0
|
|
CHB
|
B:HEM200
|
3.5
|
21.0
|
1.0
|
|
CG
|
B:MET52
|
3.6
|
16.5
|
1.0
|
|
CG
|
A:MET52
|
3.8
|
20.5
|
1.0
|
|
C3D
|
B:HEM200
|
4.2
|
29.5
|
1.0
|
|
C2D
|
B:HEM200
|
4.2
|
30.1
|
1.0
|
|
C3C
|
B:HEM200
|
4.3
|
24.4
|
1.0
|
|
C2A
|
B:HEM200
|
4.3
|
32.2
|
1.0
|
|
C3A
|
B:HEM200
|
4.3
|
28.6
|
1.0
|
|
C2C
|
B:HEM200
|
4.3
|
23.2
|
1.0
|
|
C3B
|
B:HEM200
|
4.4
|
30.9
|
1.0
|
|
C2B
|
B:HEM200
|
4.4
|
30.1
|
1.0
|
|
CB
|
B:MET52
|
4.4
|
23.1
|
1.0
|
|
CB
|
A:MET52
|
4.5
|
21.7
|
1.0
|
|
Iron binding site 2 out
of 24 in 3uoi
Go back to
Iron Binding Sites List in 3uoi
Iron binding site 2 out
of 24 in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Mycobacterium Tuberculosis Bacterioferritin, Bfra within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe200
b:31.8
occ:1.00
|
FE
|
C:HEM200
|
0.0
|
31.8
|
1.0
|
|
ND
|
C:HEM200
|
1.5
|
31.3
|
1.0
|
|
NA
|
C:HEM200
|
1.9
|
23.9
|
1.0
|
|
NB
|
C:HEM200
|
2.3
|
18.8
|
1.0
|
|
SD
|
C:MET52
|
2.3
|
24.9
|
1.0
|
|
NC
|
C:HEM200
|
2.3
|
33.6
|
1.0
|
|
C1D
|
C:HEM200
|
2.6
|
33.7
|
1.0
|
|
SD
|
D:MET52
|
2.6
|
22.7
|
1.0
|
|
C4D
|
C:HEM200
|
2.7
|
26.2
|
1.0
|
|
C1A
|
C:HEM200
|
2.9
|
28.7
|
1.0
|
|
C4A
|
C:HEM200
|
2.9
|
23.6
|
1.0
|
|
CE
|
D:MET52
|
3.0
|
17.1
|
1.0
|
|
CHA
|
C:HEM200
|
3.1
|
27.6
|
1.0
|
|
CE
|
C:MET52
|
3.3
|
22.7
|
1.0
|
|
C1C
|
C:HEM200
|
3.3
|
32.9
|
1.0
|
|
C4B
|
C:HEM200
|
3.3
|
25.9
|
1.0
|
|
C1B
|
C:HEM200
|
3.4
|
24.1
|
1.0
|
|
C4C
|
C:HEM200
|
3.4
|
33.6
|
1.0
|
|
CG
|
C:MET52
|
3.4
|
17.6
|
1.0
|
|
CHD
|
C:HEM200
|
3.4
|
33.6
|
1.0
|
|
CHB
|
C:HEM200
|
3.6
|
29.3
|
1.0
|
|
CG
|
D:MET52
|
3.6
|
17.4
|
1.0
|
|
CHC
|
C:HEM200
|
3.7
|
26.9
|
1.0
|
|
C2D
|
C:HEM200
|
3.8
|
33.1
|
1.0
|
|
C3D
|
C:HEM200
|
3.8
|
31.8
|
1.0
|
|
C2A
|
C:HEM200
|
4.1
|
31.4
|
1.0
|
|
C3A
|
C:HEM200
|
4.1
|
30.9
|
1.0
|
|
CB
|
C:MET52
|
4.3
|
24.3
|
1.0
|
|
CB
|
D:MET52
|
4.5
|
22.9
|
1.0
|
|
C3B
|
C:HEM200
|
4.6
|
25.3
|
1.0
|
|
C2C
|
C:HEM200
|
4.6
|
38.3
|
1.0
|
|
C2B
|
C:HEM200
|
4.6
|
26.2
|
1.0
|
|
C3C
|
C:HEM200
|
4.6
|
38.3
|
1.0
|
|
Iron binding site 3 out
of 24 in 3uoi
Go back to
Iron Binding Sites List in 3uoi
Iron binding site 3 out
of 24 in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Mycobacterium Tuberculosis Bacterioferritin, Bfra within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe200
b:24.9
occ:1.00
|
FE
|
F:HEM200
|
0.0
|
24.9
|
1.0
|
|
NA
|
F:HEM200
|
2.0
|
28.5
|
1.0
|
|
ND
|
F:HEM200
|
2.1
|
30.4
|
1.0
|
|
NB
|
F:HEM200
|
2.1
|
24.4
|
1.0
|
|
NC
|
F:HEM200
|
2.2
|
27.4
|
1.0
|
|
SD
|
E:MET52
|
2.2
|
21.7
|
1.0
|
|
SD
|
F:MET52
|
2.5
|
23.7
|
1.0
|
|
C1A
|
F:HEM200
|
2.8
|
33.8
|
1.0
|
|
C4D
|
F:HEM200
|
2.9
|
32.5
|
1.0
|
|
C4A
|
F:HEM200
|
3.0
|
31.6
|
1.0
|
|
C4B
|
F:HEM200
|
3.1
|
25.1
|
1.0
|
|
C1B
|
F:HEM200
|
3.1
|
26.3
|
1.0
|
|
CHA
|
F:HEM200
|
3.1
|
29.2
|
1.0
|
|
C1D
|
F:HEM200
|
3.1
|
23.6
|
1.0
|
|
C1C
|
F:HEM200
|
3.2
|
25.2
|
1.0
|
|
C4C
|
F:HEM200
|
3.2
|
19.2
|
1.0
|
|
CE
|
E:MET52
|
3.3
|
12.4
|
1.0
|
|
CE
|
F:MET52
|
3.3
|
13.8
|
1.0
|
|
CHC
|
F:HEM200
|
3.4
|
23.4
|
1.0
|
|
CHB
|
F:HEM200
|
3.5
|
26.8
|
1.0
|
|
CHD
|
F:HEM200
|
3.5
|
20.3
|
1.0
|
|
CG
|
E:MET52
|
3.6
|
20.3
|
1.0
|
|
CG
|
F:MET52
|
3.6
|
23.4
|
1.0
|
|
C2A
|
F:HEM200
|
4.1
|
35.5
|
1.0
|
|
C3A
|
F:HEM200
|
4.2
|
34.2
|
1.0
|
|
C3D
|
F:HEM200
|
4.2
|
34.4
|
1.0
|
|
C3B
|
F:HEM200
|
4.3
|
26.4
|
1.0
|
|
C2B
|
F:HEM200
|
4.3
|
28.4
|
1.0
|
|
C2D
|
F:HEM200
|
4.3
|
30.8
|
1.0
|
|
C3C
|
F:HEM200
|
4.4
|
24.2
|
1.0
|
|
CB
|
E:MET52
|
4.4
|
18.5
|
1.0
|
|
C2C
|
F:HEM200
|
4.4
|
25.5
|
1.0
|
|
CB
|
F:MET52
|
4.4
|
19.2
|
1.0
|
|
Iron binding site 4 out
of 24 in 3uoi
Go back to
Iron Binding Sites List in 3uoi
Iron binding site 4 out
of 24 in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Mycobacterium Tuberculosis Bacterioferritin, Bfra within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Fe200
b:23.4
occ:1.00
|
FE
|
H:HEM200
|
0.0
|
23.4
|
1.0
|
|
NA
|
H:HEM200
|
2.1
|
24.3
|
1.0
|
|
NC
|
H:HEM200
|
2.1
|
24.0
|
1.0
|
|
ND
|
H:HEM200
|
2.1
|
27.7
|
1.0
|
|
NB
|
H:HEM200
|
2.2
|
24.7
|
1.0
|
|
SD
|
G:MET52
|
2.3
|
26.1
|
1.0
|
|
SD
|
H:MET52
|
2.5
|
20.2
|
1.0
|
|
C1A
|
H:HEM200
|
3.0
|
22.4
|
1.0
|
|
C4C
|
H:HEM200
|
3.1
|
23.2
|
1.0
|
|
C4A
|
H:HEM200
|
3.1
|
23.9
|
1.0
|
|
C4D
|
H:HEM200
|
3.1
|
26.9
|
1.0
|
|
C1D
|
H:HEM200
|
3.1
|
23.4
|
1.0
|
|
C1C
|
H:HEM200
|
3.1
|
27.5
|
1.0
|
|
C1B
|
H:HEM200
|
3.1
|
20.1
|
1.0
|
|
CE
|
H:MET52
|
3.2
|
15.5
|
1.0
|
|
C4B
|
H:HEM200
|
3.2
|
25.6
|
1.0
|
|
CHD
|
H:HEM200
|
3.4
|
25.6
|
1.0
|
|
CHA
|
H:HEM200
|
3.4
|
24.2
|
1.0
|
|
CG
|
G:MET52
|
3.5
|
20.4
|
1.0
|
|
CHB
|
H:HEM200
|
3.5
|
23.4
|
1.0
|
|
CHC
|
H:HEM200
|
3.5
|
24.7
|
1.0
|
|
CE
|
G:MET52
|
3.7
|
17.6
|
1.0
|
|
CG
|
H:MET52
|
3.9
|
13.9
|
1.0
|
|
C2A
|
H:HEM200
|
4.2
|
23.0
|
1.0
|
|
C3A
|
H:HEM200
|
4.3
|
21.2
|
1.0
|
|
C3C
|
H:HEM200
|
4.3
|
25.1
|
1.0
|
|
C3D
|
H:HEM200
|
4.3
|
30.9
|
1.0
|
|
C2C
|
H:HEM200
|
4.3
|
27.8
|
1.0
|
|
CB
|
G:MET52
|
4.3
|
22.0
|
1.0
|
|
C2D
|
H:HEM200
|
4.3
|
26.5
|
1.0
|
|
C2B
|
H:HEM200
|
4.4
|
24.0
|
1.0
|
|
C3B
|
H:HEM200
|
4.4
|
20.2
|
1.0
|
|
CB
|
H:MET52
|
4.4
|
16.1
|
1.0
|
|
Iron binding site 5 out
of 24 in 3uoi
Go back to
Iron Binding Sites List in 3uoi
Iron binding site 5 out
of 24 in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Mycobacterium Tuberculosis Bacterioferritin, Bfra within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Fe200
b:21.0
occ:1.00
|
FE
|
I:HEM200
|
0.0
|
21.0
|
1.0
|
|
NA
|
I:HEM200
|
1.8
|
15.1
|
1.0
|
|
NC
|
I:HEM200
|
1.9
|
19.8
|
1.0
|
|
ND
|
I:HEM200
|
2.1
|
21.3
|
1.0
|
|
NB
|
I:HEM200
|
2.2
|
21.0
|
1.0
|
|
SD
|
I:MET52
|
2.4
|
23.3
|
1.0
|
|
SD
|
J:MET52
|
2.6
|
21.6
|
1.0
|
|
C1C
|
I:HEM200
|
2.9
|
18.7
|
1.0
|
|
C4C
|
I:HEM200
|
3.0
|
20.9
|
1.0
|
|
C1A
|
I:HEM200
|
3.0
|
20.9
|
1.0
|
|
C4A
|
I:HEM200
|
3.0
|
11.3
|
1.0
|
|
C1D
|
I:HEM200
|
3.0
|
17.7
|
1.0
|
|
CE
|
I:MET52
|
3.1
|
17.2
|
1.0
|
|
C4D
|
I:HEM200
|
3.1
|
25.8
|
1.0
|
|
C1B
|
I:HEM200
|
3.1
|
11.3
|
1.0
|
|
C4B
|
I:HEM200
|
3.2
|
20.4
|
1.0
|
|
CE
|
J:MET52
|
3.3
|
24.0
|
1.0
|
|
CHD
|
I:HEM200
|
3.3
|
14.6
|
1.0
|
|
CHB
|
I:HEM200
|
3.4
|
18.8
|
1.0
|
|
CHC
|
I:HEM200
|
3.4
|
21.1
|
1.0
|
|
CHA
|
I:HEM200
|
3.4
|
22.7
|
1.0
|
|
CG
|
I:MET52
|
3.5
|
14.1
|
1.0
|
|
CG
|
J:MET52
|
3.7
|
17.3
|
1.0
|
|
C2C
|
I:HEM200
|
4.1
|
19.7
|
1.0
|
|
C3C
|
I:HEM200
|
4.2
|
19.3
|
1.0
|
|
C2A
|
I:HEM200
|
4.2
|
25.0
|
1.0
|
|
C3A
|
I:HEM200
|
4.2
|
17.5
|
1.0
|
|
C2D
|
I:HEM200
|
4.2
|
22.3
|
1.0
|
|
CB
|
I:MET52
|
4.3
|
15.0
|
1.0
|
|
C3D
|
I:HEM200
|
4.3
|
26.7
|
1.0
|
|
C2B
|
I:HEM200
|
4.4
|
18.0
|
1.0
|
|
CB
|
J:MET52
|
4.4
|
17.3
|
1.0
|
|
C3B
|
I:HEM200
|
4.4
|
23.3
|
1.0
|
|
Iron binding site 6 out
of 24 in 3uoi
Go back to
Iron Binding Sites List in 3uoi
Iron binding site 6 out
of 24 in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Mycobacterium Tuberculosis Bacterioferritin, Bfra within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Fe200
b:24.6
occ:1.00
|
FE
|
L:HEM200
|
0.0
|
24.6
|
1.0
|
|
NA
|
L:HEM200
|
2.1
|
20.3
|
1.0
|
|
ND
|
L:HEM200
|
2.1
|
20.3
|
1.0
|
|
NC
|
L:HEM200
|
2.1
|
18.9
|
1.0
|
|
NB
|
L:HEM200
|
2.1
|
23.8
|
1.0
|
|
SD
|
K:MET52
|
2.4
|
29.6
|
1.0
|
|
SD
|
L:MET52
|
2.6
|
23.1
|
1.0
|
|
C1C
|
L:HEM200
|
3.0
|
19.4
|
1.0
|
|
C1A
|
L:HEM200
|
3.1
|
20.9
|
1.0
|
|
C4D
|
L:HEM200
|
3.1
|
21.1
|
1.0
|
|
C4A
|
L:HEM200
|
3.1
|
15.0
|
1.0
|
|
C4B
|
L:HEM200
|
3.1
|
17.9
|
1.0
|
|
C1D
|
L:HEM200
|
3.1
|
20.2
|
1.0
|
|
CE
|
K:MET52
|
3.2
|
27.1
|
1.0
|
|
C1B
|
L:HEM200
|
3.2
|
19.8
|
1.0
|
|
C4C
|
L:HEM200
|
3.2
|
21.1
|
1.0
|
|
CHC
|
L:HEM200
|
3.3
|
20.2
|
1.0
|
|
CE
|
L:MET52
|
3.3
|
12.6
|
1.0
|
|
CHA
|
L:HEM200
|
3.4
|
21.9
|
1.0
|
|
CG
|
L:MET52
|
3.5
|
14.2
|
1.0
|
|
CHB
|
L:HEM200
|
3.5
|
15.0
|
1.0
|
|
CG
|
K:MET52
|
3.5
|
23.0
|
1.0
|
|
CHD
|
L:HEM200
|
3.6
|
19.4
|
1.0
|
|
CB
|
L:MET52
|
4.2
|
18.2
|
1.0
|
|
C2A
|
L:HEM200
|
4.3
|
23.5
|
1.0
|
|
C2C
|
L:HEM200
|
4.3
|
27.1
|
1.0
|
|
C3A
|
L:HEM200
|
4.3
|
15.7
|
1.0
|
|
C3D
|
L:HEM200
|
4.3
|
27.7
|
1.0
|
|
C2D
|
L:HEM200
|
4.3
|
21.9
|
1.0
|
|
C3B
|
L:HEM200
|
4.4
|
23.0
|
1.0
|
|
CB
|
K:MET52
|
4.4
|
23.8
|
1.0
|
|
C3C
|
L:HEM200
|
4.4
|
21.1
|
1.0
|
|
C2B
|
L:HEM200
|
4.4
|
18.3
|
1.0
|
|
Iron binding site 7 out
of 24 in 3uoi
Go back to
Iron Binding Sites List in 3uoi
Iron binding site 7 out
of 24 in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Mycobacterium Tuberculosis Bacterioferritin, Bfra within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Fe200
b:23.1
occ:1.00
|
FE
|
M:HEM200
|
0.0
|
23.1
|
1.0
|
|
NC
|
M:HEM200
|
2.0
|
23.4
|
1.0
|
|
NA
|
M:HEM200
|
2.0
|
18.3
|
1.0
|
|
ND
|
M:HEM200
|
2.1
|
23.5
|
1.0
|
|
NB
|
M:HEM200
|
2.1
|
19.9
|
1.0
|
|
SD
|
M:MET52
|
2.5
|
26.2
|
1.0
|
|
SD
|
N:MET52
|
2.5
|
28.3
|
1.0
|
|
C1A
|
M:HEM200
|
3.0
|
22.4
|
1.0
|
|
C1C
|
M:HEM200
|
3.0
|
24.5
|
1.0
|
|
C4D
|
M:HEM200
|
3.0
|
26.1
|
1.0
|
|
C4A
|
M:HEM200
|
3.0
|
22.4
|
1.0
|
|
C4C
|
M:HEM200
|
3.1
|
25.6
|
1.0
|
|
C1B
|
M:HEM200
|
3.1
|
20.1
|
1.0
|
|
C1D
|
M:HEM200
|
3.1
|
24.4
|
1.0
|
|
C4B
|
M:HEM200
|
3.1
|
19.6
|
1.0
|
|
CE
|
N:MET52
|
3.2
|
20.0
|
1.0
|
|
CE
|
M:MET52
|
3.2
|
12.9
|
1.0
|
|
CHA
|
M:HEM200
|
3.3
|
14.5
|
1.0
|
|
CHC
|
M:HEM200
|
3.4
|
25.6
|
1.0
|
|
CHB
|
M:HEM200
|
3.4
|
18.7
|
1.0
|
|
CHD
|
M:HEM200
|
3.5
|
26.9
|
1.0
|
|
CG
|
N:MET52
|
3.5
|
18.8
|
1.0
|
|
CG
|
M:MET52
|
3.6
|
12.1
|
1.0
|
|
C2A
|
M:HEM200
|
4.2
|
25.3
|
1.0
|
|
C3A
|
M:HEM200
|
4.2
|
24.9
|
1.0
|
|
C2C
|
M:HEM200
|
4.2
|
26.3
|
1.0
|
|
C3C
|
M:HEM200
|
4.3
|
26.1
|
1.0
|
|
C3D
|
M:HEM200
|
4.3
|
29.1
|
1.0
|
|
C2D
|
M:HEM200
|
4.3
|
27.4
|
1.0
|
|
C2B
|
M:HEM200
|
4.3
|
19.6
|
1.0
|
|
C3B
|
M:HEM200
|
4.4
|
17.8
|
1.0
|
|
CB
|
N:MET52
|
4.4
|
19.7
|
1.0
|
|
CB
|
M:MET52
|
4.5
|
20.3
|
1.0
|
|
Iron binding site 8 out
of 24 in 3uoi
Go back to
Iron Binding Sites List in 3uoi
Iron binding site 8 out
of 24 in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Mycobacterium Tuberculosis Bacterioferritin, Bfra within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
P:Fe200
b:25.0
occ:1.00
|
FE
|
P:HEM200
|
0.0
|
25.0
|
1.0
|
|
NA
|
P:HEM200
|
1.8
|
27.2
|
1.0
|
|
NB
|
P:HEM200
|
2.0
|
25.9
|
1.0
|
|
NC
|
P:HEM200
|
2.0
|
24.4
|
1.0
|
|
ND
|
P:HEM200
|
2.0
|
22.6
|
1.0
|
|
SD
|
P:MET52
|
2.4
|
22.2
|
1.0
|
|
SD
|
O:MET52
|
2.6
|
25.8
|
1.0
|
|
C1A
|
P:HEM200
|
2.9
|
29.0
|
1.0
|
|
C4A
|
P:HEM200
|
2.9
|
26.8
|
1.0
|
|
C1C
|
P:HEM200
|
3.0
|
21.1
|
1.0
|
|
C4D
|
P:HEM200
|
3.0
|
25.9
|
1.0
|
|
C4B
|
P:HEM200
|
3.0
|
22.3
|
1.0
|
|
C1B
|
P:HEM200
|
3.1
|
24.1
|
1.0
|
|
C4C
|
P:HEM200
|
3.1
|
12.2
|
1.0
|
|
C1D
|
P:HEM200
|
3.1
|
16.1
|
1.0
|
|
CE
|
O:MET52
|
3.2
|
13.7
|
1.0
|
|
CE
|
P:MET52
|
3.3
|
17.4
|
1.0
|
|
CHA
|
P:HEM200
|
3.3
|
28.3
|
1.0
|
|
CHC
|
P:HEM200
|
3.4
|
20.3
|
1.0
|
|
CHB
|
P:HEM200
|
3.4
|
24.8
|
1.0
|
|
CHD
|
P:HEM200
|
3.5
|
17.7
|
1.0
|
|
CG
|
O:MET52
|
3.6
|
22.6
|
1.0
|
|
CG
|
P:MET52
|
3.7
|
7.0
|
1.0
|
|
C2A
|
P:HEM200
|
4.1
|
33.3
|
1.0
|
|
C3A
|
P:HEM200
|
4.1
|
28.3
|
1.0
|
|
C2C
|
P:HEM200
|
4.2
|
17.1
|
1.0
|
|
C3B
|
P:HEM200
|
4.2
|
19.2
|
1.0
|
|
C2B
|
P:HEM200
|
4.2
|
21.5
|
1.0
|
|
C3C
|
P:HEM200
|
4.3
|
19.2
|
1.0
|
|
C3D
|
P:HEM200
|
4.3
|
29.5
|
1.0
|
|
CB
|
P:MET52
|
4.3
|
16.1
|
1.0
|
|
C2D
|
P:HEM200
|
4.3
|
25.5
|
1.0
|
|
CB
|
O:MET52
|
4.4
|
23.5
|
1.0
|
|
Iron binding site 9 out
of 24 in 3uoi
Go back to
Iron Binding Sites List in 3uoi
Iron binding site 9 out
of 24 in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Mycobacterium Tuberculosis Bacterioferritin, Bfra within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
R:Fe200
b:23.4
occ:1.00
|
FE
|
R:HEM200
|
0.0
|
23.4
|
1.0
|
|
NC
|
R:HEM200
|
1.9
|
29.8
|
1.0
|
|
NB
|
R:HEM200
|
2.2
|
25.6
|
1.0
|
|
ND
|
R:HEM200
|
2.2
|
24.8
|
1.0
|
|
NA
|
R:HEM200
|
2.2
|
28.9
|
1.0
|
|
SD
|
Q:MET52
|
2.2
|
24.4
|
1.0
|
|
SD
|
R:MET52
|
2.6
|
27.3
|
1.0
|
|
C1C
|
R:HEM200
|
2.9
|
31.8
|
1.0
|
|
C4C
|
R:HEM200
|
3.0
|
27.4
|
1.0
|
|
C4B
|
R:HEM200
|
3.1
|
28.6
|
1.0
|
|
C1A
|
R:HEM200
|
3.1
|
24.7
|
1.0
|
|
C4D
|
R:HEM200
|
3.1
|
27.4
|
1.0
|
|
C1D
|
R:HEM200
|
3.1
|
22.2
|
1.0
|
|
CE
|
Q:MET52
|
3.2
|
17.7
|
1.0
|
|
C4A
|
R:HEM200
|
3.2
|
28.4
|
1.0
|
|
C1B
|
R:HEM200
|
3.2
|
28.1
|
1.0
|
|
CE
|
R:MET52
|
3.3
|
16.4
|
1.0
|
|
CHC
|
R:HEM200
|
3.3
|
30.3
|
1.0
|
|
CHA
|
R:HEM200
|
3.4
|
29.8
|
1.0
|
|
CHD
|
R:HEM200
|
3.4
|
28.1
|
1.0
|
|
CHB
|
R:HEM200
|
3.6
|
28.0
|
1.0
|
|
CG
|
R:MET52
|
3.7
|
22.5
|
1.0
|
|
CG
|
Q:MET52
|
3.8
|
18.3
|
1.0
|
|
C2C
|
R:HEM200
|
4.1
|
33.6
|
1.0
|
|
C3C
|
R:HEM200
|
4.1
|
33.9
|
1.0
|
|
CB
|
R:MET52
|
4.3
|
21.7
|
1.0
|
|
C2D
|
R:HEM200
|
4.3
|
26.6
|
1.0
|
|
C3D
|
R:HEM200
|
4.3
|
25.3
|
1.0
|
|
C3B
|
R:HEM200
|
4.3
|
23.0
|
1.0
|
|
C2A
|
R:HEM200
|
4.3
|
29.9
|
1.0
|
|
C3A
|
R:HEM200
|
4.4
|
30.8
|
1.0
|
|
CB
|
Q:MET52
|
4.4
|
23.2
|
1.0
|
|
C2B
|
R:HEM200
|
4.4
|
28.4
|
1.0
|
|
Iron binding site 10 out
of 24 in 3uoi
Go back to
Iron Binding Sites List in 3uoi
Iron binding site 10 out
of 24 in the Mycobacterium Tuberculosis Bacterioferritin, Bfra
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Mycobacterium Tuberculosis Bacterioferritin, Bfra within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe200
b:18.8
occ:1.00
|
FE
|
S:HEM200
|
0.0
|
18.8
|
1.0
|
|
NA
|
S:HEM200
|
1.9
|
12.2
|
1.0
|
|
NB
|
S:HEM200
|
1.9
|
19.9
|
1.0
|
|
ND
|
S:HEM200
|
2.0
|
16.6
|
1.0
|
|
NC
|
S:HEM200
|
2.1
|
15.6
|
1.0
|
|
SD
|
T:MET52
|
2.5
|
16.3
|
1.0
|
|
SD
|
S:MET52
|
2.6
|
17.6
|
1.0
|
|
C1A
|
S:HEM200
|
2.8
|
15.6
|
1.0
|
|
C4B
|
S:HEM200
|
2.9
|
19.7
|
1.0
|
|
C1C
|
S:HEM200
|
3.0
|
17.2
|
1.0
|
|
C4D
|
S:HEM200
|
3.0
|
12.9
|
1.0
|
|
C4A
|
S:HEM200
|
3.0
|
12.6
|
1.0
|
|
C1B
|
S:HEM200
|
3.0
|
19.0
|
1.0
|
|
C1D
|
S:HEM200
|
3.1
|
13.9
|
1.0
|
|
C4C
|
S:HEM200
|
3.1
|
11.1
|
1.0
|
|
CHA
|
S:HEM200
|
3.2
|
18.3
|
1.0
|
|
CHC
|
S:HEM200
|
3.2
|
14.7
|
1.0
|
|
CE
|
T:MET52
|
3.3
|
6.8
|
1.0
|
|
CHD
|
S:HEM200
|
3.5
|
12.5
|
1.0
|
|
CE
|
S:MET52
|
3.5
|
4.7
|
1.0
|
|
CHB
|
S:HEM200
|
3.6
|
10.7
|
1.0
|
|
CG
|
T:MET52
|
3.7
|
12.8
|
1.0
|
|
CG
|
S:MET52
|
3.8
|
19.4
|
1.0
|
|
C2A
|
S:HEM200
|
4.1
|
18.5
|
1.0
|
|
C3B
|
S:HEM200
|
4.1
|
15.4
|
1.0
|
|
C3A
|
S:HEM200
|
4.1
|
12.6
|
1.0
|
|
C2B
|
S:HEM200
|
4.2
|
14.8
|
1.0
|
|
C2D
|
S:HEM200
|
4.2
|
17.5
|
1.0
|
|
C2C
|
S:HEM200
|
4.3
|
15.4
|
1.0
|
|
C3D
|
S:HEM200
|
4.3
|
19.9
|
1.0
|
|
CB
|
T:MET52
|
4.3
|
14.9
|
1.0
|
|
C3C
|
S:HEM200
|
4.3
|
16.6
|
1.0
|
|
CB
|
S:MET52
|
4.4
|
16.2
|
1.0
|
|
Reference:
L.M.Mcmath,
C.W.Goulding.
Mycobacterium Tuberculosis Bacterioferritin, Bfra To Be Published.
Page generated: Sun Aug 4 21:16:20 2024
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