Iron in PDB 8bhx: High Resolution Structure of the Iron Superoxide Dismutase From Thermobifida Fusca
Enzymatic activity of High Resolution Structure of the Iron Superoxide Dismutase From Thermobifida Fusca
All present enzymatic activity of High Resolution Structure of the Iron Superoxide Dismutase From Thermobifida Fusca:
1.15.1.1;
Protein crystallography data
The structure of High Resolution Structure of the Iron Superoxide Dismutase From Thermobifida Fusca, PDB code: 8bhx
was solved by
H.-K.S.Leiros,
M.Sorlie,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
24.65 /
1.25
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
98.61,
58.59,
67.94,
90,
90,
90
|
R / Rfree (%)
|
12.5 /
14.5
|
Iron Binding Sites:
The binding sites of Iron atom in the High Resolution Structure of the Iron Superoxide Dismutase From Thermobifida Fusca
(pdb code 8bhx). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
High Resolution Structure of the Iron Superoxide Dismutase From Thermobifida Fusca, PDB code: 8bhx:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 8bhx
Go back to
Iron Binding Sites List in 8bhx
Iron binding site 1 out
of 2 in the High Resolution Structure of the Iron Superoxide Dismutase From Thermobifida Fusca
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of High Resolution Structure of the Iron Superoxide Dismutase From Thermobifida Fusca within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:8.2
occ:0.77
|
OD2
|
A:ASP161
|
2.0
|
9.9
|
1.0
|
O
|
A:HOH533
|
2.1
|
10.8
|
1.0
|
NE2
|
A:HIS77
|
2.2
|
10.6
|
1.0
|
NE2
|
A:HIS29
|
2.2
|
9.6
|
1.0
|
NE2
|
A:HIS165
|
2.2
|
10.5
|
1.0
|
O
|
A:HOH421
|
2.2
|
15.6
|
0.7
|
CE1
|
A:HIS77
|
3.0
|
10.4
|
1.0
|
CG
|
A:ASP161
|
3.1
|
9.0
|
1.0
|
CE1
|
A:HIS29
|
3.1
|
9.2
|
1.0
|
CE1
|
A:HIS165
|
3.2
|
11.1
|
1.0
|
CD2
|
A:HIS29
|
3.2
|
9.6
|
1.0
|
HE1
|
A:HIS77
|
3.2
|
12.4
|
1.0
|
CD2
|
A:HIS165
|
3.2
|
9.9
|
1.0
|
CD2
|
A:HIS77
|
3.2
|
9.5
|
1.0
|
HE1
|
A:HIS29
|
3.3
|
11.1
|
1.0
|
HE1
|
A:HIS165
|
3.3
|
13.3
|
1.0
|
HD2
|
A:HIS29
|
3.3
|
11.6
|
1.0
|
HD2
|
A:HIS165
|
3.4
|
11.9
|
1.0
|
HD2
|
A:HIS77
|
3.4
|
11.4
|
1.0
|
OD1
|
A:ASP161
|
3.5
|
9.8
|
1.0
|
HB2
|
A:TRP163
|
3.8
|
8.9
|
1.0
|
HE1
|
A:HIS146
|
4.0
|
10.8
|
1.0
|
HZ2
|
A:TRP126
|
4.0
|
11.3
|
1.0
|
HB2
|
A:ALA166
|
4.1
|
12.6
|
1.0
|
HE1
|
A:TYR37
|
4.1
|
15.9
|
1.0
|
ND1
|
A:HIS77
|
4.2
|
10.3
|
1.0
|
ND1
|
A:HIS29
|
4.2
|
10.9
|
1.0
|
ND1
|
A:HIS165
|
4.3
|
11.3
|
1.0
|
CG
|
A:HIS29
|
4.3
|
10.0
|
1.0
|
CG
|
A:HIS77
|
4.3
|
10.1
|
1.0
|
CG
|
A:HIS165
|
4.3
|
9.7
|
1.0
|
HH2
|
A:TRP126
|
4.3
|
9.7
|
1.0
|
CB
|
A:ASP161
|
4.4
|
8.8
|
1.0
|
HB2
|
A:ASP161
|
4.4
|
10.6
|
1.0
|
CZ2
|
A:TRP126
|
4.5
|
9.4
|
1.0
|
HB3
|
A:ASP161
|
4.6
|
10.6
|
1.0
|
CB
|
A:TRP163
|
4.6
|
7.4
|
1.0
|
CH2
|
A:TRP126
|
4.6
|
8.1
|
1.0
|
HB3
|
A:HIS33
|
4.6
|
12.9
|
1.0
|
CG
|
A:TRP163
|
4.8
|
8.1
|
1.0
|
OH
|
A:TYR37
|
4.8
|
25.5
|
1.0
|
HB3
|
A:TRP163
|
4.9
|
8.9
|
1.0
|
HB2
|
A:HIS33
|
4.9
|
12.9
|
1.0
|
CE1
|
A:HIS146
|
4.9
|
9.0
|
1.0
|
HD1
|
A:HIS77
|
5.0
|
12.4
|
1.0
|
CE1
|
A:TYR37
|
5.0
|
13.2
|
1.0
|
|
Iron binding site 2 out
of 2 in 8bhx
Go back to
Iron Binding Sites List in 8bhx
Iron binding site 2 out
of 2 in the High Resolution Structure of the Iron Superoxide Dismutase From Thermobifida Fusca
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of High Resolution Structure of the Iron Superoxide Dismutase From Thermobifida Fusca within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe301
b:8.5
occ:0.93
|
OD2
|
B:ASP161
|
2.0
|
8.0
|
1.0
|
O
|
B:HOH553
|
2.1
|
9.0
|
1.0
|
O
|
B:HOH433
|
2.1
|
18.1
|
1.0
|
NE2
|
B:HIS29
|
2.2
|
7.9
|
1.0
|
NE2
|
B:HIS77
|
2.2
|
9.6
|
1.0
|
NE2
|
B:HIS165
|
2.2
|
10.4
|
1.0
|
CE1
|
B:HIS77
|
3.0
|
9.9
|
1.0
|
CG
|
B:ASP161
|
3.1
|
7.7
|
1.0
|
CE1
|
B:HIS29
|
3.1
|
7.5
|
1.0
|
HE1
|
B:HIS77
|
3.1
|
11.9
|
1.0
|
CD2
|
B:HIS29
|
3.1
|
7.4
|
1.0
|
CE1
|
B:HIS165
|
3.2
|
10.9
|
1.0
|
CD2
|
B:HIS165
|
3.2
|
9.1
|
1.0
|
CD2
|
B:HIS77
|
3.3
|
8.8
|
1.0
|
HE1
|
B:HIS29
|
3.3
|
9.0
|
1.0
|
HD2
|
B:HIS29
|
3.3
|
8.8
|
1.0
|
HE1
|
B:HIS165
|
3.3
|
13.1
|
1.0
|
HD2
|
B:HIS165
|
3.4
|
10.9
|
1.0
|
HD2
|
B:HIS77
|
3.5
|
10.6
|
1.0
|
OD1
|
B:ASP161
|
3.5
|
8.2
|
1.0
|
HB2
|
B:TRP163
|
3.8
|
9.3
|
1.0
|
HE1
|
B:HIS146
|
4.0
|
9.3
|
1.0
|
HZ2
|
B:TRP126
|
4.0
|
10.1
|
1.0
|
HB2
|
B:ALA166
|
4.0
|
10.1
|
1.0
|
ND1
|
B:HIS77
|
4.2
|
8.5
|
1.0
|
OH
|
B:TYR37
|
4.2
|
9.9
|
0.5
|
ND1
|
B:HIS29
|
4.2
|
8.9
|
1.0
|
HE2
|
B:TYR37
|
4.3
|
9.4
|
0.5
|
CG
|
B:HIS29
|
4.3
|
8.7
|
1.0
|
HE2
|
B:TYR37
|
4.3
|
8.6
|
0.5
|
ND1
|
B:HIS165
|
4.3
|
9.8
|
1.0
|
CB
|
B:ASP161
|
4.3
|
7.0
|
1.0
|
CG
|
B:HIS165
|
4.3
|
8.5
|
1.0
|
CG
|
B:HIS77
|
4.3
|
8.6
|
1.0
|
HH2
|
B:TRP126
|
4.4
|
10.8
|
1.0
|
HB2
|
B:ASP161
|
4.4
|
8.4
|
1.0
|
CZ2
|
B:TRP126
|
4.5
|
8.4
|
1.0
|
HH
|
B:TYR37
|
4.5
|
11.1
|
0.5
|
HB3
|
B:ASP161
|
4.6
|
8.4
|
1.0
|
CB
|
B:TRP163
|
4.6
|
7.8
|
1.0
|
HB3
|
B:HIS33
|
4.6
|
9.8
|
1.0
|
CH2
|
B:TRP126
|
4.7
|
9.0
|
1.0
|
HH
|
B:TYR37
|
4.7
|
11.8
|
0.5
|
CG
|
B:TRP163
|
4.8
|
7.0
|
1.0
|
CE1
|
B:HIS146
|
4.9
|
7.7
|
1.0
|
HB3
|
B:TRP163
|
4.9
|
9.3
|
1.0
|
HB2
|
B:HIS33
|
4.9
|
9.8
|
1.0
|
HD1
|
B:HIS77
|
5.0
|
10.2
|
1.0
|
CB
|
B:ALA166
|
5.0
|
8.4
|
1.0
|
HD1
|
B:HIS29
|
5.0
|
10.7
|
1.0
|
|
Reference:
A.G.Hamre,
R.Al-Sadawi,
K.M.Johannesen,
B.Bisarro,
A.R.Kjendseth,
H.S.Leiros,
M.Sorlie.
Initial Characterization of An Iron Superoxide Dismutase From Thermobifida Fusca. J.Biol.Inorg.Chem. 2023.
ISSN: ESSN 1432-1327
PubMed: 37725277
DOI: 10.1007/S00775-023-02019-9
Page generated: Fri Aug 9 19:54:28 2024
|