Iron in PDB 5nku: Joint Neutron/X-Ray Structure of Dimeric Chlorite Dismutase From Cyanothece Sp. PCC7425
Protein crystallography data
The structure of Joint Neutron/X-Ray Structure of Dimeric Chlorite Dismutase From Cyanothece Sp. PCC7425, PDB code: 5nku
was solved by
D.Puehringer,
I.Schaffner,
G.Mlynek,
C.Obinger,
K.Djinovic-Carugo,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
N/A /
2.00
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
52.427,
53.015,
55.337,
107.30,
98.54,
109.86
|
R / Rfree (%)
|
23.9 /
25.3
|
Other elements in 5nku:
The structure of Joint Neutron/X-Ray Structure of Dimeric Chlorite Dismutase From Cyanothece Sp. PCC7425 also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Joint Neutron/X-Ray Structure of Dimeric Chlorite Dismutase From Cyanothece Sp. PCC7425
(pdb code 5nku). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Joint Neutron/X-Ray Structure of Dimeric Chlorite Dismutase From Cyanothece Sp. PCC7425, PDB code: 5nku:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 5nku
Go back to
Iron Binding Sites List in 5nku
Iron binding site 1 out
of 2 in the Joint Neutron/X-Ray Structure of Dimeric Chlorite Dismutase From Cyanothece Sp. PCC7425
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Joint Neutron/X-Ray Structure of Dimeric Chlorite Dismutase From Cyanothece Sp. PCC7425 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe500
b:37.6
occ:1.00
|
FE
|
A:HEM500
|
0.0
|
37.6
|
1.0
|
NA
|
A:HEM500
|
1.9
|
32.9
|
1.0
|
NC
|
A:HEM500
|
2.0
|
38.8
|
1.0
|
NB
|
A:HEM500
|
2.1
|
41.0
|
1.0
|
NE2
|
A:HIS114
|
2.1
|
41.3
|
1.0
|
ND
|
A:HEM500
|
2.1
|
31.3
|
1.0
|
O
|
A:OH501
|
2.4
|
42.5
|
1.0
|
C1A
|
A:HEM500
|
2.9
|
38.1
|
1.0
|
C1C
|
A:HEM500
|
3.0
|
40.0
|
1.0
|
C4D
|
A:HEM500
|
3.0
|
25.1
|
1.0
|
HO
|
A:OH501
|
3.0
|
51.0
|
0.6
|
C4B
|
A:HEM500
|
3.0
|
37.4
|
1.0
|
CD2
|
A:HIS114
|
3.0
|
39.2
|
1.0
|
CE1
|
A:HIS114
|
3.1
|
37.6
|
1.0
|
C4A
|
A:HEM500
|
3.1
|
33.7
|
1.0
|
DO
|
A:OH501
|
3.1
|
51.0
|
0.4
|
C1B
|
A:HEM500
|
3.1
|
34.1
|
1.0
|
C4C
|
A:HEM500
|
3.1
|
44.5
|
1.0
|
C1D
|
A:HEM500
|
3.1
|
35.6
|
1.0
|
HD2
|
A:HIS114
|
3.2
|
47.1
|
1.0
|
CHA
|
A:HEM500
|
3.2
|
31.3
|
1.0
|
HE1
|
A:HIS114
|
3.3
|
45.1
|
1.0
|
CHC
|
A:HEM500
|
3.3
|
33.3
|
1.0
|
CHB
|
A:HEM500
|
3.5
|
35.1
|
1.0
|
CHD
|
A:HEM500
|
3.6
|
35.8
|
1.0
|
ND1
|
A:HIS114
|
4.1
|
43.9
|
1.0
|
CG
|
A:HIS114
|
4.2
|
42.6
|
1.0
|
C2A
|
A:HEM500
|
4.2
|
38.5
|
1.0
|
C2C
|
A:HEM500
|
4.2
|
32.3
|
1.0
|
HHA
|
A:HEM500
|
4.2
|
37.6
|
1.0
|
C3A
|
A:HEM500
|
4.2
|
40.1
|
1.0
|
C3D
|
A:HEM500
|
4.2
|
33.2
|
1.0
|
HHC
|
A:HEM500
|
4.3
|
40.0
|
1.0
|
C3B
|
A:HEM500
|
4.3
|
44.3
|
1.0
|
C3C
|
A:HEM500
|
4.3
|
35.9
|
1.0
|
C2D
|
A:HEM500
|
4.3
|
31.1
|
1.0
|
C2B
|
A:HEM500
|
4.3
|
38.2
|
1.0
|
HD2
|
A:ARG127
|
4.4
|
89.4
|
1.0
|
D1
|
A:HOH604
|
4.4
|
71.0
|
1.0
|
HHB
|
A:HEM500
|
4.4
|
42.1
|
1.0
|
HZ
|
A:PHE145
|
4.5
|
49.0
|
1.0
|
O
|
A:HOH604
|
4.5
|
59.1
|
1.0
|
HHD
|
A:HEM500
|
4.5
|
42.9
|
1.0
|
HE1
|
A:PHE108
|
4.7
|
49.7
|
1.0
|
HE
|
A:ARG127
|
4.8
|
94.0
|
0.0
|
DE
|
A:ARG127
|
4.8
|
94.0
|
1.0
|
HZ
|
A:PHE108
|
4.8
|
51.7
|
1.0
|
HE1
|
A:PHE145
|
4.8
|
61.2
|
1.0
|
HE3
|
A:MET162
|
4.9
|
82.1
|
1.0
|
HD1
|
A:HIS114
|
4.9
|
52.7
|
0.0
|
DD1
|
A:HIS114
|
4.9
|
52.7
|
1.0
|
HG21
|
A:THR143
|
4.9
|
48.2
|
1.0
|
|
Iron binding site 2 out
of 2 in 5nku
Go back to
Iron Binding Sites List in 5nku
Iron binding site 2 out
of 2 in the Joint Neutron/X-Ray Structure of Dimeric Chlorite Dismutase From Cyanothece Sp. PCC7425
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Joint Neutron/X-Ray Structure of Dimeric Chlorite Dismutase From Cyanothece Sp. PCC7425 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe203
b:31.4
occ:1.00
|
FE
|
B:HEM203
|
0.0
|
31.4
|
1.0
|
NA
|
B:HEM203
|
1.9
|
25.8
|
1.0
|
NB
|
B:HEM203
|
1.9
|
32.2
|
1.0
|
NC
|
B:HEM203
|
2.0
|
31.4
|
1.0
|
ND
|
B:HEM203
|
2.0
|
29.4
|
1.0
|
NE2
|
B:HIS114
|
2.2
|
29.0
|
1.0
|
O
|
B:OH204
|
2.2
|
34.6
|
1.0
|
DO
|
B:OH204
|
2.7
|
41.5
|
1.0
|
C1B
|
B:HEM203
|
2.9
|
33.3
|
1.0
|
C4A
|
B:HEM203
|
3.0
|
29.8
|
1.0
|
C4B
|
B:HEM203
|
3.0
|
30.9
|
1.0
|
C1A
|
B:HEM203
|
3.0
|
32.4
|
1.0
|
C1C
|
B:HEM203
|
3.0
|
31.2
|
1.0
|
C1D
|
B:HEM203
|
3.1
|
26.9
|
1.0
|
C4C
|
B:HEM203
|
3.1
|
33.2
|
1.0
|
C4D
|
B:HEM203
|
3.1
|
27.3
|
1.0
|
CE1
|
B:HIS114
|
3.1
|
30.0
|
1.0
|
HO
|
B:OH204
|
3.1
|
41.5
|
0.0
|
CD2
|
B:HIS114
|
3.2
|
32.6
|
1.0
|
HE1
|
B:HIS114
|
3.2
|
36.0
|
1.0
|
CHB
|
B:HEM203
|
3.4
|
35.5
|
1.0
|
CHC
|
B:HEM203
|
3.4
|
28.6
|
1.0
|
HD2
|
B:HIS114
|
3.4
|
39.1
|
1.0
|
CHA
|
B:HEM203
|
3.4
|
30.9
|
1.0
|
CHD
|
B:HEM203
|
3.5
|
24.6
|
1.0
|
HE1
|
B:MET162
|
3.7
|
0.9
|
1.0
|
C2B
|
B:HEM203
|
4.1
|
35.0
|
1.0
|
C3B
|
B:HEM203
|
4.2
|
34.2
|
1.0
|
C3A
|
B:HEM203
|
4.2
|
36.3
|
1.0
|
C2A
|
B:HEM203
|
4.2
|
32.9
|
1.0
|
ND1
|
B:HIS114
|
4.2
|
35.2
|
1.0
|
D1
|
B:HOH308
|
4.3
|
58.4
|
1.0
|
C3D
|
B:HEM203
|
4.3
|
28.5
|
1.0
|
C2D
|
B:HEM203
|
4.3
|
31.8
|
1.0
|
HHB
|
B:HEM203
|
4.3
|
42.6
|
1.0
|
CG
|
B:HIS114
|
4.3
|
30.3
|
1.0
|
C2C
|
B:HEM203
|
4.3
|
31.7
|
1.0
|
C3C
|
B:HEM203
|
4.3
|
31.9
|
1.0
|
HHC
|
B:HEM203
|
4.4
|
34.4
|
1.0
|
HHA
|
B:HEM203
|
4.4
|
37.1
|
1.0
|
HHD
|
B:HEM203
|
4.4
|
29.6
|
1.0
|
D2
|
B:HOH308
|
4.4
|
58.4
|
1.0
|
HD2
|
B:ARG127
|
4.5
|
62.1
|
1.0
|
O
|
B:HOH308
|
4.5
|
48.7
|
1.0
|
HZ
|
B:PHE145
|
4.6
|
34.8
|
1.0
|
HE1
|
B:PHE108
|
4.6
|
36.3
|
1.0
|
DE
|
B:ARG127
|
4.6
|
69.8
|
1.0
|
CE
|
B:MET162
|
4.6
|
0.2
|
1.0
|
HE1
|
B:PHE145
|
4.8
|
46.2
|
1.0
|
HE3
|
B:MET162
|
4.8
|
0.9
|
1.0
|
HE
|
B:ARG127
|
4.9
|
69.8
|
0.0
|
HG21
|
B:THR143
|
4.9
|
43.1
|
1.0
|
HD1
|
B:HIS114
|
5.0
|
42.2
|
0.0
|
DD1
|
B:HIS114
|
5.0
|
42.2
|
1.0
|
|
Reference:
I.Schaffner,
G.Mlynek,
N.Flego,
D.Puhringer,
J.Libiseller-Egger,
L.Coates,
S.Hofbauer,
M.Bellei,
P.G.Furtmuller,
G.Battistuzzi,
G.Smulevich,
K.Djinovic-Carugo,
C.Obinger.
Molecular Mechanism of Enzymatic Chlorite Detoxification: Insights From Structural and Kinetic Studies. Acs Catal V. 7 7962 2017.
ISSN: ESSN 2155-5435
PubMed: 29142780
DOI: 10.1021/ACSCATAL.7B01749
Page generated: Tue Aug 6 06:13:12 2024
|