Iron in PDB 4e1h: Fragment of Human Prion Protein
Protein crystallography data
The structure of Fragment of Human Prion Protein, PDB code: 4e1h
was solved by
M.I.Apostol,
K.Perry,
W.K.Surewicz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
22.55 /
1.40
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
32.317,
42.898,
46.353,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.4 /
21.8
|
Iron Binding Sites:
The binding sites of Iron atom in the Fragment of Human Prion Protein
(pdb code 4e1h). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the
Fragment of Human Prion Protein, PDB code: 4e1h:
Jump to Iron binding site number:
1;
2;
3;
Iron binding site 1 out
of 3 in 4e1h
Go back to
Iron Binding Sites List in 4e1h
Iron binding site 1 out
of 3 in the Fragment of Human Prion Protein
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Fragment of Human Prion Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Fe201
b:19.4
occ:1.00
|
O7
|
G:CIT202
|
2.0
|
16.1
|
1.0
|
O6
|
I:CIT203
|
2.0
|
20.0
|
1.0
|
O7
|
G:CIT203
|
2.0
|
19.9
|
1.0
|
O4
|
G:CIT202
|
2.0
|
21.7
|
1.0
|
O4
|
G:CIT203
|
2.1
|
22.0
|
1.0
|
O6
|
G:CIT203
|
2.2
|
24.6
|
1.0
|
C3
|
G:CIT203
|
2.9
|
21.3
|
1.0
|
C6
|
G:CIT203
|
2.9
|
26.0
|
1.0
|
C5
|
G:CIT202
|
3.0
|
24.0
|
1.0
|
O7
|
I:CIT203
|
3.0
|
18.9
|
1.0
|
C6
|
I:CIT203
|
3.0
|
18.4
|
1.0
|
C5
|
G:CIT203
|
3.0
|
26.0
|
1.0
|
C3
|
G:CIT202
|
3.1
|
18.2
|
1.0
|
C4
|
G:CIT202
|
3.4
|
18.5
|
1.0
|
FE
|
I:FE202
|
3.4
|
18.7
|
1.0
|
FE
|
I:FE201
|
3.4
|
19.0
|
1.0
|
C4
|
G:CIT203
|
3.5
|
24.0
|
1.0
|
C2
|
G:CIT202
|
3.6
|
20.7
|
1.0
|
C3
|
I:CIT203
|
3.6
|
18.1
|
1.0
|
O2
|
G:CIT202
|
3.8
|
30.7
|
1.0
|
O7
|
I:CIT204
|
3.9
|
18.7
|
1.0
|
O2
|
I:CIT203
|
4.0
|
20.9
|
1.0
|
O5
|
I:CIT203
|
4.1
|
23.1
|
1.0
|
O5
|
G:CIT203
|
4.1
|
31.3
|
1.0
|
O3
|
I:CIT203
|
4.1
|
21.4
|
1.0
|
O3
|
G:CIT203
|
4.1
|
33.9
|
1.0
|
C2
|
G:CIT203
|
4.1
|
23.5
|
1.0
|
O3
|
G:CIT202
|
4.2
|
29.0
|
1.0
|
C1
|
G:CIT202
|
4.2
|
25.2
|
1.0
|
C6
|
G:CIT202
|
4.3
|
21.5
|
1.0
|
C5
|
I:CIT203
|
4.4
|
19.8
|
1.0
|
O6
|
G:CIT202
|
4.6
|
21.3
|
1.0
|
C1
|
I:CIT203
|
4.6
|
19.6
|
1.0
|
O1
|
G:CIT203
|
4.6
|
21.5
|
1.0
|
C4
|
I:CIT203
|
4.6
|
19.6
|
1.0
|
CB
|
G:HIS177
|
4.7
|
34.4
|
1.0
|
C2
|
I:CIT203
|
4.7
|
19.7
|
1.0
|
CD2
|
G:HIS177
|
4.8
|
37.6
|
1.0
|
CG
|
G:HIS177
|
4.9
|
34.7
|
1.0
|
C1
|
G:CIT203
|
4.9
|
22.7
|
1.0
|
|
Iron binding site 2 out
of 3 in 4e1h
Go back to
Iron Binding Sites List in 4e1h
Iron binding site 2 out
of 3 in the Fragment of Human Prion Protein
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Fragment of Human Prion Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Fe201
b:19.0
occ:1.00
|
O1
|
G:CIT203
|
2.0
|
21.5
|
1.0
|
O2
|
I:CIT203
|
2.0
|
20.9
|
1.0
|
O7
|
G:CIT203
|
2.0
|
19.9
|
1.0
|
O7
|
I:CIT203
|
2.0
|
18.9
|
1.0
|
O7
|
I:CIT204
|
2.0
|
18.7
|
1.0
|
O2
|
I:CIT204
|
2.1
|
23.7
|
1.0
|
C1
|
I:CIT204
|
2.9
|
23.1
|
1.0
|
C1
|
I:CIT203
|
2.9
|
19.6
|
1.0
|
C1
|
G:CIT203
|
3.0
|
22.7
|
1.0
|
C3
|
I:CIT203
|
3.1
|
18.1
|
1.0
|
FE
|
I:FE202
|
3.1
|
18.7
|
1.0
|
C3
|
I:CIT204
|
3.1
|
22.4
|
1.0
|
C3
|
G:CIT203
|
3.2
|
21.3
|
1.0
|
C2
|
I:CIT204
|
3.2
|
21.8
|
1.0
|
C2
|
I:CIT203
|
3.3
|
19.7
|
1.0
|
C2
|
G:CIT203
|
3.4
|
23.5
|
1.0
|
FE
|
G:FE201
|
3.4
|
19.4
|
1.0
|
O7
|
G:CIT202
|
3.7
|
16.1
|
1.0
|
C4
|
G:CIT203
|
3.7
|
24.0
|
1.0
|
C6
|
I:CIT203
|
3.8
|
18.4
|
1.0
|
C6
|
I:CIT204
|
3.8
|
22.2
|
1.0
|
O6
|
I:CIT203
|
3.9
|
20.0
|
1.0
|
O6
|
I:CIT204
|
4.0
|
23.9
|
1.0
|
O1
|
I:CIT204
|
4.0
|
25.8
|
1.0
|
O3
|
I:CIT204
|
4.1
|
29.3
|
1.0
|
O1
|
I:CIT203
|
4.1
|
23.6
|
1.0
|
O2
|
G:CIT203
|
4.2
|
26.9
|
1.0
|
O4
|
G:CIT203
|
4.2
|
22.0
|
1.0
|
C5
|
G:CIT203
|
4.2
|
26.0
|
1.0
|
C4
|
I:CIT203
|
4.3
|
19.6
|
1.0
|
C4
|
I:CIT204
|
4.4
|
25.8
|
1.0
|
O2
|
G:CIT202
|
4.4
|
30.7
|
1.0
|
C6
|
G:CIT203
|
4.4
|
26.0
|
1.0
|
C5
|
I:CIT204
|
4.6
|
28.6
|
1.0
|
O3
|
I:CIT203
|
4.6
|
21.4
|
1.0
|
O6
|
G:CIT203
|
4.7
|
24.6
|
1.0
|
O5
|
I:CIT204
|
4.8
|
27.9
|
1.0
|
O5
|
I:CIT203
|
4.8
|
23.1
|
1.0
|
O6
|
G:CIT202
|
4.9
|
21.3
|
1.0
|
C5
|
I:CIT203
|
5.0
|
19.8
|
1.0
|
|
Iron binding site 3 out
of 3 in 4e1h
Go back to
Iron Binding Sites List in 4e1h
Iron binding site 3 out
of 3 in the Fragment of Human Prion Protein
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Fragment of Human Prion Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Fe202
b:18.7
occ:1.00
|
O7
|
I:CIT203
|
1.9
|
18.9
|
1.0
|
O3
|
I:CIT203
|
2.0
|
21.4
|
1.0
|
O7
|
G:CIT202
|
2.0
|
16.1
|
1.0
|
O6
|
G:CIT202
|
2.0
|
21.3
|
1.0
|
O6
|
I:CIT204
|
2.1
|
23.9
|
1.0
|
O7
|
I:CIT204
|
2.1
|
18.7
|
1.0
|
C6
|
G:CIT202
|
2.8
|
21.5
|
1.0
|
C6
|
I:CIT204
|
2.8
|
22.2
|
1.0
|
C5
|
I:CIT203
|
2.9
|
19.8
|
1.0
|
C3
|
G:CIT202
|
2.9
|
18.2
|
1.0
|
C3
|
I:CIT204
|
2.9
|
22.4
|
1.0
|
C3
|
I:CIT203
|
3.0
|
18.1
|
1.0
|
FE
|
I:FE201
|
3.1
|
19.0
|
1.0
|
C4
|
I:CIT203
|
3.3
|
19.6
|
1.0
|
FE
|
G:FE201
|
3.4
|
19.4
|
1.0
|
O7
|
G:CIT203
|
3.6
|
19.9
|
1.0
|
O6
|
I:CIT203
|
3.6
|
20.0
|
1.0
|
C4
|
I:CIT204
|
3.7
|
25.8
|
1.0
|
O2
|
G:CIT202
|
3.8
|
30.7
|
1.0
|
C4
|
G:CIT202
|
3.8
|
18.5
|
1.0
|
C6
|
I:CIT203
|
3.8
|
18.4
|
1.0
|
O5
|
G:CIT202
|
3.9
|
24.0
|
1.0
|
O2
|
I:CIT204
|
4.0
|
23.7
|
1.0
|
O5
|
I:CIT204
|
4.0
|
27.9
|
1.0
|
O4
|
I:CIT203
|
4.1
|
21.7
|
1.0
|
C1
|
G:CIT202
|
4.1
|
25.2
|
1.0
|
C2
|
G:CIT202
|
4.1
|
20.7
|
1.0
|
C2
|
I:CIT204
|
4.2
|
21.8
|
1.0
|
C2
|
I:CIT203
|
4.2
|
19.7
|
1.0
|
C1
|
I:CIT204
|
4.5
|
23.1
|
1.0
|
O4
|
G:CIT202
|
4.5
|
21.7
|
1.0
|
C5
|
I:CIT204
|
4.6
|
28.6
|
1.0
|
O2
|
I:CIT203
|
4.6
|
20.9
|
1.0
|
C5
|
G:CIT202
|
4.7
|
24.0
|
1.0
|
O1
|
G:CIT203
|
4.8
|
21.5
|
1.0
|
O3
|
I:CIT204
|
4.8
|
29.3
|
1.0
|
O6
|
G:CIT203
|
4.9
|
24.6
|
1.0
|
C3
|
G:CIT203
|
4.9
|
21.3
|
1.0
|
C1
|
I:CIT203
|
4.9
|
19.6
|
1.0
|
O1
|
G:CIT202
|
4.9
|
29.0
|
1.0
|
|
Reference:
M.I.Apostol,
K.Perry,
W.K.Surewicz.
Crystal Structure of A Human Prion Protein Fragment Reveals A Motif For Oligomer Formation. J.Am.Chem.Soc. V. 135 10202 2013.
ISSN: ISSN 0002-7863
PubMed: 23808589
DOI: 10.1021/JA403001Q
Page generated: Mon Aug 5 01:29:52 2024
|