Iron in PDB 1ft5: Crystal Structure of the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea
Protein crystallography data
The structure of Crystal Structure of the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea, PDB code: 1ft5
was solved by
T.M.Iverson,
D.M.Arciero,
A.B.Hooper,
D.C.Rees,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
1.60
|
Space group
|
H 3
|
Cell size a, b, c (Å), α, β, γ (°)
|
147.892,
147.892,
33.913,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
18.8 /
21.5
|
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea
(pdb code 1ft5). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Crystal Structure of the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea, PDB code: 1ft5:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 1ft5
Go back to
Iron Binding Sites List in 1ft5
Iron binding site 1 out
of 4 in the Crystal Structure of the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea
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 the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe213
b:16.1
occ:1.00
|
FE
|
A:HEM213
|
0.0
|
16.1
|
1.0
|
NE2
|
A:HIS15
|
1.9
|
17.9
|
1.0
|
ND
|
A:HEM213
|
2.0
|
14.4
|
1.0
|
NC
|
A:HEM213
|
2.0
|
19.5
|
1.0
|
NB
|
A:HEM213
|
2.0
|
13.9
|
1.0
|
NA
|
A:HEM213
|
2.0
|
16.4
|
1.0
|
ND1
|
A:HIS102
|
2.1
|
17.9
|
1.0
|
C4D
|
A:HEM213
|
3.0
|
16.2
|
1.0
|
CE1
|
A:HIS15
|
3.0
|
15.2
|
1.0
|
C1D
|
A:HEM213
|
3.0
|
20.9
|
1.0
|
C1A
|
A:HEM213
|
3.0
|
16.1
|
1.0
|
CE1
|
A:HIS102
|
3.0
|
13.2
|
1.0
|
C4C
|
A:HEM213
|
3.0
|
20.5
|
1.0
|
C1C
|
A:HEM213
|
3.0
|
18.6
|
1.0
|
C1B
|
A:HEM213
|
3.0
|
17.9
|
1.0
|
C4B
|
A:HEM213
|
3.1
|
17.3
|
1.0
|
CD2
|
A:HIS15
|
3.1
|
13.6
|
1.0
|
C4A
|
A:HEM213
|
3.1
|
18.3
|
1.0
|
CG
|
A:HIS102
|
3.2
|
18.5
|
1.0
|
CHA
|
A:HEM213
|
3.4
|
18.6
|
1.0
|
CHD
|
A:HEM213
|
3.4
|
16.6
|
1.0
|
CHB
|
A:HEM213
|
3.5
|
16.2
|
1.0
|
CHC
|
A:HEM213
|
3.5
|
17.8
|
1.0
|
CB
|
A:HIS102
|
3.6
|
16.2
|
1.0
|
ND1
|
A:HIS15
|
4.1
|
17.1
|
1.0
|
C3D
|
A:HEM213
|
4.2
|
18.0
|
1.0
|
C2D
|
A:HEM213
|
4.2
|
18.9
|
1.0
|
CG
|
A:HIS15
|
4.2
|
16.8
|
1.0
|
NE2
|
A:HIS102
|
4.2
|
17.0
|
1.0
|
C3C
|
A:HEM213
|
4.2
|
19.0
|
1.0
|
C2B
|
A:HEM213
|
4.3
|
16.0
|
1.0
|
C3A
|
A:HEM213
|
4.3
|
17.6
|
1.0
|
C2A
|
A:HEM213
|
4.3
|
16.3
|
1.0
|
C3B
|
A:HEM213
|
4.3
|
16.6
|
1.0
|
C2C
|
A:HEM213
|
4.3
|
21.8
|
1.0
|
CD2
|
A:HIS102
|
4.3
|
18.5
|
1.0
|
|
Iron binding site 2 out
of 4 in 1ft5
Go back to
Iron Binding Sites List in 1ft5
Iron binding site 2 out
of 4 in the Crystal Structure of the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea
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 the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe214
b:12.1
occ:1.00
|
FE
|
A:HEM214
|
0.0
|
12.1
|
1.0
|
NC
|
A:HEM214
|
2.0
|
11.8
|
1.0
|
NB
|
A:HEM214
|
2.0
|
11.7
|
1.0
|
ND
|
A:HEM214
|
2.0
|
10.2
|
1.0
|
NA
|
A:HEM214
|
2.0
|
12.4
|
1.0
|
NE2
|
A:HIS64
|
2.2
|
11.0
|
1.0
|
CE1
|
A:HIS64
|
3.0
|
11.7
|
1.0
|
C4C
|
A:HEM214
|
3.0
|
9.6
|
1.0
|
C1D
|
A:HEM214
|
3.1
|
12.8
|
1.0
|
C4D
|
A:HEM214
|
3.1
|
13.7
|
1.0
|
C1C
|
A:HEM214
|
3.1
|
12.1
|
1.0
|
C1B
|
A:HEM214
|
3.1
|
11.1
|
1.0
|
C4B
|
A:HEM214
|
3.1
|
10.8
|
1.0
|
C4A
|
A:HEM214
|
3.1
|
14.0
|
1.0
|
C1A
|
A:HEM214
|
3.1
|
11.0
|
1.0
|
CD2
|
A:HIS64
|
3.3
|
13.3
|
1.0
|
CHD
|
A:HEM214
|
3.4
|
11.3
|
1.0
|
CHA
|
A:HEM214
|
3.5
|
10.8
|
1.0
|
CHB
|
A:HEM214
|
3.5
|
11.8
|
1.0
|
CHC
|
A:HEM214
|
3.5
|
11.9
|
1.0
|
CD1
|
A:PHE156
|
4.1
|
17.7
|
1.0
|
CE1
|
A:PHE156
|
4.2
|
19.1
|
1.0
|
ND1
|
A:HIS64
|
4.2
|
11.0
|
1.0
|
C2D
|
A:HEM214
|
4.3
|
12.6
|
1.0
|
C3C
|
A:HEM214
|
4.3
|
10.0
|
1.0
|
C3D
|
A:HEM214
|
4.3
|
12.2
|
1.0
|
C2C
|
A:HEM214
|
4.3
|
11.4
|
1.0
|
C3B
|
A:HEM214
|
4.3
|
12.4
|
1.0
|
C2B
|
A:HEM214
|
4.3
|
14.0
|
1.0
|
C2A
|
A:HEM214
|
4.3
|
11.7
|
1.0
|
C3A
|
A:HEM214
|
4.4
|
13.4
|
1.0
|
CD
|
A:PRO155
|
4.4
|
14.8
|
1.0
|
CG
|
A:HIS64
|
4.4
|
10.7
|
1.0
|
CMD
|
A:HEM216
|
4.5
|
11.8
|
1.0
|
OG1
|
A:THR154
|
4.6
|
14.2
|
1.0
|
|
Iron binding site 3 out
of 4 in 1ft5
Go back to
Iron Binding Sites List in 1ft5
Iron binding site 3 out
of 4 in the Crystal Structure of the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure of the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe215
b:13.8
occ:1.00
|
FE
|
A:HEM215
|
0.0
|
13.8
|
1.0
|
ND
|
A:HEM215
|
2.0
|
16.9
|
1.0
|
NB
|
A:HEM215
|
2.0
|
15.3
|
1.0
|
NA
|
A:HEM215
|
2.0
|
12.4
|
1.0
|
NC
|
A:HEM215
|
2.0
|
10.2
|
1.0
|
NE2
|
A:HIS179
|
2.0
|
16.1
|
1.0
|
NE2
|
A:HIS92
|
2.0
|
11.0
|
1.0
|
CE1
|
A:HIS92
|
3.0
|
10.1
|
1.0
|
C1C
|
A:HEM215
|
3.0
|
16.6
|
1.0
|
CE1
|
A:HIS179
|
3.0
|
16.3
|
1.0
|
C1A
|
A:HEM215
|
3.0
|
16.5
|
1.0
|
C4B
|
A:HEM215
|
3.0
|
12.4
|
1.0
|
CD2
|
A:HIS179
|
3.0
|
14.1
|
1.0
|
C4D
|
A:HEM215
|
3.0
|
13.0
|
1.0
|
C4A
|
A:HEM215
|
3.0
|
16.9
|
1.0
|
C4C
|
A:HEM215
|
3.0
|
14.2
|
1.0
|
C1B
|
A:HEM215
|
3.1
|
15.2
|
1.0
|
C1D
|
A:HEM215
|
3.1
|
15.0
|
1.0
|
CD2
|
A:HIS92
|
3.1
|
13.3
|
1.0
|
CHA
|
A:HEM215
|
3.4
|
17.5
|
1.0
|
CHC
|
A:HEM215
|
3.4
|
13.5
|
1.0
|
CHD
|
A:HEM215
|
3.4
|
15.9
|
1.0
|
CHB
|
A:HEM215
|
3.5
|
15.5
|
1.0
|
ND1
|
A:HIS92
|
4.2
|
15.5
|
1.0
|
ND1
|
A:HIS179
|
4.2
|
14.2
|
1.0
|
CG
|
A:HIS179
|
4.2
|
16.4
|
1.0
|
C2A
|
A:HEM215
|
4.2
|
15.2
|
1.0
|
C2C
|
A:HEM215
|
4.2
|
12.8
|
1.0
|
CG
|
A:HIS92
|
4.2
|
12.4
|
1.0
|
C3C
|
A:HEM215
|
4.2
|
12.2
|
1.0
|
C3A
|
A:HEM215
|
4.2
|
13.7
|
1.0
|
C2B
|
A:HEM215
|
4.3
|
14.3
|
1.0
|
C3D
|
A:HEM215
|
4.3
|
14.2
|
1.0
|
C3B
|
A:HEM215
|
4.3
|
14.0
|
1.0
|
C2D
|
A:HEM215
|
4.3
|
14.3
|
1.0
|
|
Iron binding site 4 out
of 4 in 1ft5
Go back to
Iron Binding Sites List in 1ft5
Iron binding site 4 out
of 4 in the Crystal Structure of the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure of the Oxidized State of Cytochrome C554 From Nitrosomonas Europaea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe216
b:12.5
occ:1.00
|
FE
|
A:HEM216
|
0.0
|
12.5
|
1.0
|
NB
|
A:HEM216
|
1.9
|
13.3
|
1.0
|
NA
|
A:HEM216
|
2.0
|
11.1
|
1.0
|
NE2
|
A:HIS27
|
2.0
|
12.0
|
1.0
|
NC
|
A:HEM216
|
2.0
|
11.8
|
1.0
|
ND
|
A:HEM216
|
2.0
|
11.5
|
1.0
|
NE2
|
A:HIS138
|
2.0
|
12.5
|
1.0
|
CE1
|
A:HIS27
|
2.9
|
13.3
|
1.0
|
CE1
|
A:HIS138
|
3.0
|
14.8
|
1.0
|
C1A
|
A:HEM216
|
3.0
|
13.3
|
1.0
|
C4D
|
A:HEM216
|
3.0
|
11.8
|
1.0
|
C4A
|
A:HEM216
|
3.0
|
14.8
|
1.0
|
C1C
|
A:HEM216
|
3.0
|
12.1
|
1.0
|
C1D
|
A:HEM216
|
3.0
|
11.5
|
1.0
|
C4B
|
A:HEM216
|
3.0
|
11.4
|
1.0
|
C4C
|
A:HEM216
|
3.0
|
13.3
|
1.0
|
CD2
|
A:HIS27
|
3.0
|
11.1
|
1.0
|
C1B
|
A:HEM216
|
3.0
|
12.2
|
1.0
|
CD2
|
A:HIS138
|
3.1
|
10.3
|
1.0
|
CHA
|
A:HEM216
|
3.4
|
13.2
|
1.0
|
CHB
|
A:HEM216
|
3.4
|
15.1
|
1.0
|
CHD
|
A:HEM216
|
3.4
|
10.8
|
1.0
|
CHC
|
A:HEM216
|
3.4
|
10.8
|
1.0
|
ND1
|
A:HIS27
|
4.1
|
12.7
|
1.0
|
ND1
|
A:HIS138
|
4.1
|
12.1
|
1.0
|
CG
|
A:HIS27
|
4.2
|
13.0
|
1.0
|
C2A
|
A:HEM216
|
4.2
|
12.9
|
1.0
|
C3A
|
A:HEM216
|
4.2
|
13.7
|
1.0
|
CG
|
A:HIS138
|
4.2
|
10.8
|
1.0
|
C2D
|
A:HEM216
|
4.2
|
10.6
|
1.0
|
C3D
|
A:HEM216
|
4.2
|
11.6
|
1.0
|
C3C
|
A:HEM216
|
4.3
|
10.8
|
1.0
|
C2B
|
A:HEM216
|
4.3
|
12.6
|
1.0
|
C2C
|
A:HEM216
|
4.3
|
11.6
|
1.0
|
C3B
|
A:HEM216
|
4.3
|
13.1
|
1.0
|
|
Reference:
T.M.Iverson,
D.M.Arciero,
A.B.Hooper,
D.C.Rees.
High-Resolution Structures of the Oxidized and Reduced States of Cytochrome C554 From Nitrosomonas Europaea. J.Biol.Inorg.Chem. V. 6 390 2001.
ISSN: ISSN 0949-8257
PubMed: 11372197
DOI: 10.1007/S007750100213
Page generated: Sat Aug 3 05:27:34 2024
|