Iron in PDB 5o0t: Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)
Protein crystallography data
The structure of Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5), PDB code: 5o0t
was solved by
F.Magnani,
S.Nenci,
A.Mattevi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
44.60 /
2.05
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
52.371,
74.570,
85.120,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.5 /
22.1
|
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)
(pdb code 5o0t). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5), PDB code: 5o0t:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 5o0t
Go back to
Iron Binding Sites List in 5o0t
Iron binding site 1 out
of 2 in the Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe504
b:24.3
occ:1.00
|
FE
|
A:HEM504
|
0.0
|
24.3
|
1.0
|
ND
|
A:HEM504
|
1.9
|
26.0
|
1.0
|
NA
|
A:HEM504
|
2.0
|
25.8
|
1.0
|
NE2
|
A:HIS299
|
2.0
|
25.1
|
1.0
|
NE2
|
A:HIS372
|
2.0
|
25.4
|
1.0
|
NB
|
A:HEM504
|
2.1
|
27.2
|
1.0
|
NC
|
A:HEM504
|
2.1
|
25.1
|
1.0
|
C1D
|
A:HEM504
|
2.9
|
26.6
|
1.0
|
C4D
|
A:HEM504
|
2.9
|
26.3
|
1.0
|
CE1
|
A:HIS372
|
2.9
|
24.4
|
1.0
|
CE1
|
A:HIS299
|
3.0
|
24.2
|
1.0
|
C4A
|
A:HEM504
|
3.0
|
27.6
|
1.0
|
C1A
|
A:HEM504
|
3.0
|
26.3
|
1.0
|
CD2
|
A:HIS299
|
3.0
|
24.3
|
1.0
|
C4B
|
A:HEM504
|
3.0
|
26.4
|
1.0
|
C1B
|
A:HEM504
|
3.0
|
27.6
|
1.0
|
C4C
|
A:HEM504
|
3.1
|
26.2
|
1.0
|
CD2
|
A:HIS372
|
3.1
|
25.9
|
1.0
|
C1C
|
A:HEM504
|
3.1
|
25.0
|
1.0
|
CHD
|
A:HEM504
|
3.4
|
25.8
|
1.0
|
CHB
|
A:HEM504
|
3.4
|
25.9
|
1.0
|
CHA
|
A:HEM504
|
3.4
|
25.4
|
1.0
|
CHC
|
A:HEM504
|
3.5
|
25.8
|
1.0
|
ND1
|
A:HIS372
|
4.1
|
26.1
|
1.0
|
ND1
|
A:HIS299
|
4.1
|
22.6
|
1.0
|
C2D
|
A:HEM504
|
4.2
|
27.7
|
1.0
|
CG
|
A:HIS299
|
4.2
|
24.1
|
1.0
|
C3D
|
A:HEM504
|
4.2
|
29.8
|
1.0
|
CG
|
A:HIS372
|
4.2
|
27.0
|
1.0
|
C3A
|
A:HEM504
|
4.2
|
29.7
|
1.0
|
C2A
|
A:HEM504
|
4.2
|
31.4
|
1.0
|
C2B
|
A:HEM504
|
4.3
|
27.6
|
1.0
|
C3B
|
A:HEM504
|
4.3
|
30.8
|
1.0
|
C3C
|
A:HEM504
|
4.3
|
28.0
|
1.0
|
C2C
|
A:HEM504
|
4.3
|
27.4
|
1.0
|
|
Iron binding site 2 out
of 2 in 5o0t
Go back to
Iron Binding Sites List in 5o0t
Iron binding site 2 out
of 2 in the Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5)
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure of Trans-Membrane Domain of Cylindrospermum Stagnale Nadph-Oxidase 5 (NOX5) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe505
b:23.5
occ:1.00
|
FE
|
A:HEM505
|
0.0
|
23.5
|
1.0
|
NE2
|
A:HIS385
|
1.9
|
26.0
|
1.0
|
ND
|
A:HEM505
|
1.9
|
24.8
|
1.0
|
NE2
|
A:HIS313
|
2.0
|
25.0
|
1.0
|
NA
|
A:HEM505
|
2.0
|
24.7
|
1.0
|
NC
|
A:HEM505
|
2.1
|
24.8
|
1.0
|
NB
|
A:HEM505
|
2.1
|
24.0
|
1.0
|
CE1
|
A:HIS385
|
2.9
|
25.8
|
1.0
|
CE1
|
A:HIS313
|
3.0
|
23.7
|
1.0
|
C1D
|
A:HEM505
|
3.0
|
24.9
|
1.0
|
C4D
|
A:HEM505
|
3.0
|
24.2
|
1.0
|
CD2
|
A:HIS385
|
3.0
|
25.4
|
1.0
|
C1A
|
A:HEM505
|
3.0
|
25.0
|
1.0
|
CD2
|
A:HIS313
|
3.0
|
23.7
|
1.0
|
C4B
|
A:HEM505
|
3.0
|
25.2
|
1.0
|
C4C
|
A:HEM505
|
3.1
|
24.3
|
1.0
|
C4A
|
A:HEM505
|
3.1
|
26.6
|
1.0
|
C1B
|
A:HEM505
|
3.1
|
25.4
|
1.0
|
C1C
|
A:HEM505
|
3.1
|
24.8
|
1.0
|
CHA
|
A:HEM505
|
3.4
|
23.5
|
1.0
|
CHD
|
A:HEM505
|
3.4
|
22.3
|
1.0
|
CHC
|
A:HEM505
|
3.4
|
22.8
|
1.0
|
CHB
|
A:HEM505
|
3.5
|
25.0
|
1.0
|
ND1
|
A:HIS385
|
4.0
|
24.1
|
1.0
|
ND1
|
A:HIS313
|
4.1
|
23.2
|
1.0
|
CG
|
A:HIS385
|
4.1
|
25.2
|
1.0
|
CG
|
A:HIS313
|
4.1
|
23.2
|
1.0
|
C2A
|
A:HEM505
|
4.2
|
26.6
|
1.0
|
C2D
|
A:HEM505
|
4.2
|
24.6
|
1.0
|
C3D
|
A:HEM505
|
4.3
|
27.4
|
1.0
|
C3A
|
A:HEM505
|
4.3
|
26.1
|
1.0
|
C3C
|
A:HEM505
|
4.3
|
25.3
|
1.0
|
C2C
|
A:HEM505
|
4.3
|
24.3
|
1.0
|
C2B
|
A:HEM505
|
4.3
|
25.4
|
1.0
|
C3B
|
A:HEM505
|
4.3
|
25.5
|
1.0
|
CD2
|
A:HIS317
|
4.6
|
25.4
|
1.0
|
NE2
|
A:HIS317
|
4.7
|
25.3
|
1.0
|
|
Reference:
F.Magnani,
S.Nenci,
E.Millana Fananas,
M.Ceccon,
E.Romero,
M.W.Fraaije,
A.Mattevi.
Crystal Structures and Atomic Model of Nadph Oxidase. Proc. Natl. Acad. Sci. V. 114 6764 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28607049
DOI: 10.1073/PNAS.1702293114
Page generated: Sun Dec 13 16:09:37 2020
|