Iron in PDB 1zzh: Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
Enzymatic activity of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
All present enzymatic activity of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus:
1.11.1.5;
Protein crystallography data
The structure of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus, PDB code: 1zzh
was solved by
L.De Smet,
S.N.Savvides,
E.Van Horen,
G.Pettigrew,
J.J.Vanbeeumen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.70
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
64.630,
132.470,
163.940,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
24.9 /
27.8
|
Other elements in 1zzh:
The structure of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
(pdb code 1zzh). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the
Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus, PDB code: 1zzh:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 1zzh
Go back to
Iron Binding Sites List in 1zzh
Iron binding site 1 out
of 8 in the Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe802
b:44.0
occ:1.00
|
FE
|
A:HEC802
|
0.0
|
44.0
|
1.0
|
NA
|
A:HEC802
|
1.9
|
46.1
|
1.0
|
NB
|
A:HEC802
|
1.9
|
45.4
|
1.0
|
ND
|
A:HEC802
|
2.0
|
47.6
|
1.0
|
NC
|
A:HEC802
|
2.0
|
45.5
|
1.0
|
NE2
|
A:HIS58
|
2.0
|
32.1
|
1.0
|
NE2
|
A:HIS74
|
2.3
|
44.8
|
1.0
|
C4A
|
A:HEC802
|
3.0
|
46.9
|
1.0
|
C4B
|
A:HEC802
|
3.0
|
44.8
|
1.0
|
C1A
|
A:HEC802
|
3.0
|
48.3
|
1.0
|
C1B
|
A:HEC802
|
3.0
|
45.3
|
1.0
|
CE1
|
A:HIS58
|
3.0
|
35.5
|
1.0
|
C4D
|
A:HEC802
|
3.0
|
49.1
|
1.0
|
C1C
|
A:HEC802
|
3.0
|
45.3
|
1.0
|
C4C
|
A:HEC802
|
3.0
|
46.4
|
1.0
|
C1D
|
A:HEC802
|
3.0
|
48.8
|
1.0
|
CD2
|
A:HIS58
|
3.0
|
33.9
|
1.0
|
CD2
|
A:HIS74
|
3.1
|
47.6
|
1.0
|
CE1
|
A:HIS74
|
3.3
|
48.0
|
1.0
|
CHB
|
A:HEC802
|
3.4
|
45.5
|
1.0
|
CHA
|
A:HEC802
|
3.4
|
50.0
|
1.0
|
CHC
|
A:HEC802
|
3.4
|
45.2
|
1.0
|
CHD
|
A:HEC802
|
3.4
|
48.2
|
1.0
|
ND1
|
A:HIS58
|
4.1
|
36.7
|
1.0
|
CG
|
A:HIS58
|
4.2
|
35.5
|
1.0
|
C3B
|
A:HEC802
|
4.2
|
45.0
|
1.0
|
C3A
|
A:HEC802
|
4.2
|
49.7
|
1.0
|
C2B
|
A:HEC802
|
4.3
|
44.3
|
1.0
|
C2A
|
A:HEC802
|
4.3
|
49.4
|
1.0
|
C3D
|
A:HEC802
|
4.3
|
50.3
|
1.0
|
C3C
|
A:HEC802
|
4.3
|
47.4
|
1.0
|
C2C
|
A:HEC802
|
4.3
|
45.9
|
1.0
|
C2D
|
A:HEC802
|
4.3
|
49.8
|
1.0
|
CG
|
A:HIS74
|
4.3
|
49.9
|
1.0
|
ND1
|
A:HIS74
|
4.4
|
49.8
|
1.0
|
|
Iron binding site 2 out
of 8 in 1zzh
Go back to
Iron Binding Sites List in 1zzh
Iron binding site 2 out
of 8 in the Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe803
b:42.8
occ:1.00
|
FE
|
A:HEC803
|
0.0
|
42.8
|
1.0
|
NB
|
A:HEC803
|
1.9
|
41.7
|
1.0
|
NA
|
A:HEC803
|
2.0
|
42.7
|
1.0
|
NC
|
A:HEC803
|
2.0
|
45.6
|
1.0
|
ND
|
A:HEC803
|
2.0
|
43.2
|
1.0
|
NE2
|
A:HIS204
|
2.2
|
39.9
|
1.0
|
SD
|
A:MET278
|
2.5
|
46.0
|
1.0
|
C4B
|
A:HEC803
|
3.0
|
44.5
|
1.0
|
C4A
|
A:HEC803
|
3.0
|
43.0
|
1.0
|
C1B
|
A:HEC803
|
3.0
|
41.9
|
1.0
|
C1A
|
A:HEC803
|
3.0
|
43.8
|
1.0
|
C4D
|
A:HEC803
|
3.0
|
44.4
|
1.0
|
C1C
|
A:HEC803
|
3.0
|
47.1
|
1.0
|
C4C
|
A:HEC803
|
3.0
|
46.4
|
1.0
|
C1D
|
A:HEC803
|
3.0
|
44.0
|
1.0
|
CD2
|
A:HIS204
|
3.1
|
42.9
|
1.0
|
CE1
|
A:HIS204
|
3.2
|
39.5
|
1.0
|
CHB
|
A:HEC803
|
3.4
|
43.1
|
1.0
|
CHC
|
A:HEC803
|
3.4
|
46.9
|
1.0
|
CHA
|
A:HEC803
|
3.4
|
45.0
|
1.0
|
CHD
|
A:HEC803
|
3.4
|
45.8
|
1.0
|
CG
|
A:MET278
|
3.4
|
46.5
|
1.0
|
CE
|
A:MET278
|
4.1
|
44.3
|
1.0
|
CG
|
A:HIS204
|
4.2
|
44.6
|
1.0
|
C3B
|
A:HEC803
|
4.2
|
43.6
|
1.0
|
C3A
|
A:HEC803
|
4.2
|
44.2
|
1.0
|
C2B
|
A:HEC803
|
4.2
|
42.0
|
1.0
|
ND1
|
A:HIS204
|
4.2
|
43.1
|
1.0
|
C2A
|
A:HEC803
|
4.3
|
44.5
|
1.0
|
C3D
|
A:HEC803
|
4.3
|
44.9
|
1.0
|
C3C
|
A:HEC803
|
4.3
|
48.5
|
1.0
|
C2C
|
A:HEC803
|
4.3
|
47.2
|
1.0
|
C2D
|
A:HEC803
|
4.3
|
44.4
|
1.0
|
CB
|
A:MET278
|
4.6
|
46.4
|
1.0
|
|
Iron binding site 3 out
of 8 in 1zzh
Go back to
Iron Binding Sites List in 1zzh
Iron binding site 3 out
of 8 in the Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe401
b:32.9
occ:1.00
|
FE
|
B:HEC401
|
0.0
|
32.9
|
1.0
|
NB
|
B:HEC401
|
1.9
|
33.2
|
1.0
|
NA
|
B:HEC401
|
1.9
|
34.1
|
1.0
|
ND
|
B:HEC401
|
2.0
|
34.7
|
1.0
|
NC
|
B:HEC401
|
2.0
|
34.0
|
1.0
|
NE2
|
B:HIS58
|
2.1
|
28.7
|
1.0
|
NE2
|
B:HIS74
|
2.2
|
38.8
|
1.0
|
C4A
|
B:HEC401
|
3.0
|
36.5
|
1.0
|
C4B
|
B:HEC401
|
3.0
|
34.2
|
1.0
|
C4D
|
B:HEC401
|
3.0
|
37.7
|
1.0
|
C1A
|
B:HEC401
|
3.0
|
35.2
|
1.0
|
C4C
|
B:HEC401
|
3.0
|
35.7
|
1.0
|
C1D
|
B:HEC401
|
3.0
|
35.5
|
1.0
|
C1B
|
B:HEC401
|
3.0
|
32.5
|
1.0
|
C1C
|
B:HEC401
|
3.0
|
33.1
|
1.0
|
CE1
|
B:HIS58
|
3.1
|
28.2
|
1.0
|
CD2
|
B:HIS74
|
3.1
|
38.9
|
1.0
|
CD2
|
B:HIS58
|
3.1
|
28.9
|
1.0
|
CE1
|
B:HIS74
|
3.3
|
41.3
|
1.0
|
CHB
|
B:HEC401
|
3.4
|
34.1
|
1.0
|
CHA
|
B:HEC401
|
3.4
|
37.0
|
1.0
|
CHC
|
B:HEC401
|
3.4
|
33.1
|
1.0
|
CHD
|
B:HEC401
|
3.4
|
33.9
|
1.0
|
ND1
|
B:HIS58
|
4.2
|
30.7
|
1.0
|
C3B
|
B:HEC401
|
4.2
|
35.1
|
1.0
|
CG
|
B:HIS58
|
4.2
|
29.6
|
1.0
|
C3A
|
B:HEC401
|
4.2
|
37.4
|
1.0
|
C2B
|
B:HEC401
|
4.3
|
34.0
|
1.0
|
C3D
|
B:HEC401
|
4.3
|
37.8
|
1.0
|
C2A
|
B:HEC401
|
4.3
|
36.3
|
1.0
|
C3C
|
B:HEC401
|
4.3
|
36.6
|
1.0
|
C2D
|
B:HEC401
|
4.3
|
36.9
|
1.0
|
CG
|
B:HIS74
|
4.3
|
41.2
|
1.0
|
C2C
|
B:HEC401
|
4.3
|
34.1
|
1.0
|
ND1
|
B:HIS74
|
4.3
|
41.6
|
1.0
|
|
Iron binding site 4 out
of 8 in 1zzh
Go back to
Iron Binding Sites List in 1zzh
Iron binding site 4 out
of 8 in the Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe402
b:38.9
occ:1.00
|
FE
|
B:HEC402
|
0.0
|
38.9
|
1.0
|
NB
|
B:HEC402
|
1.9
|
40.7
|
1.0
|
NA
|
B:HEC402
|
2.0
|
42.6
|
1.0
|
NC
|
B:HEC402
|
2.0
|
42.5
|
1.0
|
ND
|
B:HEC402
|
2.0
|
40.7
|
1.0
|
NE2
|
B:HIS204
|
2.2
|
42.5
|
1.0
|
SD
|
B:MET278
|
2.4
|
36.6
|
1.0
|
C4B
|
B:HEC402
|
3.0
|
41.9
|
1.0
|
C1B
|
B:HEC402
|
3.0
|
41.4
|
1.0
|
C1C
|
B:HEC402
|
3.0
|
43.3
|
1.0
|
C4A
|
B:HEC402
|
3.0
|
43.5
|
1.0
|
C4C
|
B:HEC402
|
3.0
|
43.7
|
1.0
|
C1A
|
B:HEC402
|
3.0
|
43.1
|
1.0
|
C4D
|
B:HEC402
|
3.0
|
41.0
|
1.0
|
C1D
|
B:HEC402
|
3.0
|
41.7
|
1.0
|
CD2
|
B:HIS204
|
3.1
|
41.5
|
1.0
|
CE1
|
B:HIS204
|
3.2
|
41.9
|
1.0
|
CHC
|
B:HEC402
|
3.4
|
42.1
|
1.0
|
CHB
|
B:HEC402
|
3.4
|
42.8
|
1.0
|
CG
|
B:MET278
|
3.4
|
39.6
|
1.0
|
CHA
|
B:HEC402
|
3.4
|
42.4
|
1.0
|
CHD
|
B:HEC402
|
3.4
|
42.5
|
1.0
|
CE
|
B:MET278
|
4.0
|
34.8
|
1.0
|
C3B
|
B:HEC402
|
4.2
|
41.5
|
1.0
|
C2B
|
B:HEC402
|
4.2
|
40.4
|
1.0
|
C3C
|
B:HEC402
|
4.3
|
44.9
|
1.0
|
C2C
|
B:HEC402
|
4.3
|
44.2
|
1.0
|
C3A
|
B:HEC402
|
4.3
|
44.4
|
1.0
|
C3D
|
B:HEC402
|
4.3
|
40.0
|
1.0
|
C2A
|
B:HEC402
|
4.3
|
44.2
|
1.0
|
CG
|
B:HIS204
|
4.3
|
42.3
|
1.0
|
ND1
|
B:HIS204
|
4.3
|
42.9
|
1.0
|
C2D
|
B:HEC402
|
4.3
|
41.4
|
1.0
|
CB
|
B:MET278
|
4.5
|
41.9
|
1.0
|
|
Iron binding site 5 out
of 8 in 1zzh
Go back to
Iron Binding Sites List in 1zzh
Iron binding site 5 out
of 8 in the Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe401
b:35.1
occ:1.00
|
FE
|
C:HEC401
|
0.0
|
35.1
|
1.0
|
NB
|
C:HEC401
|
1.9
|
38.1
|
1.0
|
NA
|
C:HEC401
|
2.0
|
40.0
|
1.0
|
NC
|
C:HEC401
|
2.0
|
38.2
|
1.0
|
ND
|
C:HEC401
|
2.0
|
41.1
|
1.0
|
NE2
|
C:HIS58
|
2.1
|
29.2
|
1.0
|
NE2
|
C:HIS74
|
2.2
|
38.1
|
1.0
|
C4B
|
C:HEC401
|
3.0
|
39.0
|
1.0
|
C4A
|
C:HEC401
|
3.0
|
39.4
|
1.0
|
C1C
|
C:HEC401
|
3.0
|
38.1
|
1.0
|
C4C
|
C:HEC401
|
3.0
|
39.8
|
1.0
|
C1B
|
C:HEC401
|
3.0
|
37.2
|
1.0
|
C1A
|
C:HEC401
|
3.0
|
38.7
|
1.0
|
C4D
|
C:HEC401
|
3.0
|
43.7
|
1.0
|
C1D
|
C:HEC401
|
3.0
|
40.8
|
1.0
|
CD2
|
C:HIS74
|
3.1
|
38.9
|
1.0
|
CD2
|
C:HIS58
|
3.1
|
30.4
|
1.0
|
CE1
|
C:HIS58
|
3.1
|
28.7
|
1.0
|
CE1
|
C:HIS74
|
3.3
|
41.1
|
1.0
|
CHC
|
C:HEC401
|
3.4
|
39.4
|
1.0
|
CHB
|
C:HEC401
|
3.4
|
36.9
|
1.0
|
CHD
|
C:HEC401
|
3.4
|
39.4
|
1.0
|
CHA
|
C:HEC401
|
3.4
|
41.2
|
1.0
|
ND1
|
C:HIS58
|
4.2
|
29.6
|
1.0
|
CG
|
C:HIS58
|
4.2
|
30.6
|
1.0
|
C3B
|
C:HEC401
|
4.2
|
37.5
|
1.0
|
C3A
|
C:HEC401
|
4.2
|
40.6
|
1.0
|
C3C
|
C:HEC401
|
4.3
|
41.4
|
1.0
|
C2B
|
C:HEC401
|
4.3
|
37.5
|
1.0
|
C2C
|
C:HEC401
|
4.3
|
38.5
|
1.0
|
C2A
|
C:HEC401
|
4.3
|
39.1
|
1.0
|
C3D
|
C:HEC401
|
4.3
|
44.3
|
1.0
|
CG
|
C:HIS74
|
4.3
|
41.6
|
1.0
|
C2D
|
C:HEC401
|
4.3
|
42.9
|
1.0
|
ND1
|
C:HIS74
|
4.3
|
42.9
|
1.0
|
|
Iron binding site 6 out
of 8 in 1zzh
Go back to
Iron Binding Sites List in 1zzh
Iron binding site 6 out
of 8 in the Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe402
b:36.6
occ:1.00
|
FE
|
C:HEC402
|
0.0
|
36.6
|
1.0
|
NB
|
C:HEC402
|
1.9
|
39.1
|
1.0
|
NA
|
C:HEC402
|
2.0
|
37.1
|
1.0
|
ND
|
C:HEC402
|
2.0
|
35.7
|
1.0
|
NC
|
C:HEC402
|
2.0
|
39.5
|
1.0
|
NE2
|
C:HIS204
|
2.2
|
42.3
|
1.0
|
SD
|
C:MET278
|
2.3
|
39.1
|
1.0
|
C4B
|
C:HEC402
|
3.0
|
40.9
|
1.0
|
C4A
|
C:HEC402
|
3.0
|
36.9
|
1.0
|
C1B
|
C:HEC402
|
3.0
|
40.3
|
1.0
|
C1A
|
C:HEC402
|
3.0
|
37.0
|
1.0
|
C4D
|
C:HEC402
|
3.0
|
37.7
|
1.0
|
C4C
|
C:HEC402
|
3.0
|
40.4
|
1.0
|
C1D
|
C:HEC402
|
3.0
|
37.1
|
1.0
|
C1C
|
C:HEC402
|
3.0
|
40.4
|
1.0
|
CD2
|
C:HIS204
|
3.1
|
42.5
|
1.0
|
CE1
|
C:HIS204
|
3.2
|
42.8
|
1.0
|
CHB
|
C:HEC402
|
3.4
|
38.9
|
1.0
|
CHA
|
C:HEC402
|
3.4
|
37.1
|
1.0
|
CHC
|
C:HEC402
|
3.4
|
38.8
|
1.0
|
CHD
|
C:HEC402
|
3.4
|
39.4
|
1.0
|
CG
|
C:MET278
|
3.4
|
39.1
|
1.0
|
CE
|
C:MET278
|
4.0
|
39.8
|
1.0
|
C3B
|
C:HEC402
|
4.2
|
42.0
|
1.0
|
C3D
|
C:HEC402
|
4.3
|
37.8
|
1.0
|
C3A
|
C:HEC402
|
4.3
|
37.0
|
1.0
|
CG
|
C:HIS204
|
4.3
|
43.6
|
1.0
|
C2B
|
C:HEC402
|
4.3
|
41.8
|
1.0
|
C2A
|
C:HEC402
|
4.3
|
36.8
|
1.0
|
C3C
|
C:HEC402
|
4.3
|
42.2
|
1.0
|
ND1
|
C:HIS204
|
4.3
|
43.2
|
1.0
|
C2D
|
C:HEC402
|
4.3
|
36.9
|
1.0
|
C2C
|
C:HEC402
|
4.3
|
40.9
|
1.0
|
CB
|
C:MET278
|
4.6
|
40.3
|
1.0
|
|
Iron binding site 7 out
of 8 in 1zzh
Go back to
Iron Binding Sites List in 1zzh
Iron binding site 7 out
of 8 in the Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe401
b:38.0
occ:1.00
|
FE
|
D:HEC401
|
0.0
|
38.0
|
1.0
|
NB
|
D:HEC401
|
1.9
|
38.3
|
1.0
|
NA
|
D:HEC401
|
1.9
|
39.8
|
1.0
|
ND
|
D:HEC401
|
2.0
|
41.0
|
1.0
|
NC
|
D:HEC401
|
2.0
|
38.8
|
1.0
|
NE2
|
D:HIS58
|
2.0
|
35.9
|
1.0
|
NE2
|
D:HIS74
|
2.2
|
40.9
|
1.0
|
C4B
|
D:HEC401
|
3.0
|
40.3
|
1.0
|
C4A
|
D:HEC401
|
3.0
|
41.9
|
1.0
|
C1A
|
D:HEC401
|
3.0
|
41.6
|
1.0
|
C1B
|
D:HEC401
|
3.0
|
38.0
|
1.0
|
C4D
|
D:HEC401
|
3.0
|
42.4
|
1.0
|
CE1
|
D:HIS58
|
3.0
|
36.5
|
1.0
|
C4C
|
D:HEC401
|
3.0
|
40.1
|
1.0
|
C1C
|
D:HEC401
|
3.0
|
41.1
|
1.0
|
C1D
|
D:HEC401
|
3.0
|
42.5
|
1.0
|
CD2
|
D:HIS58
|
3.0
|
34.5
|
1.0
|
CD2
|
D:HIS74
|
3.1
|
42.9
|
1.0
|
CE1
|
D:HIS74
|
3.3
|
43.1
|
1.0
|
CHB
|
D:HEC401
|
3.4
|
40.3
|
1.0
|
CHC
|
D:HEC401
|
3.4
|
42.5
|
1.0
|
CHA
|
D:HEC401
|
3.4
|
42.5
|
1.0
|
CHD
|
D:HEC401
|
3.4
|
42.8
|
1.0
|
ND1
|
D:HIS58
|
4.1
|
37.0
|
1.0
|
CG
|
D:HIS58
|
4.2
|
36.5
|
1.0
|
C3B
|
D:HEC401
|
4.2
|
38.9
|
1.0
|
C3A
|
D:HEC401
|
4.2
|
43.1
|
1.0
|
C2B
|
D:HEC401
|
4.3
|
38.7
|
1.0
|
C3C
|
D:HEC401
|
4.3
|
40.7
|
1.0
|
C3D
|
D:HEC401
|
4.3
|
43.4
|
1.0
|
C2A
|
D:HEC401
|
4.3
|
43.5
|
1.0
|
C2C
|
D:HEC401
|
4.3
|
41.5
|
1.0
|
C2D
|
D:HEC401
|
4.3
|
42.4
|
1.0
|
CG
|
D:HIS74
|
4.3
|
46.4
|
1.0
|
ND1
|
D:HIS74
|
4.4
|
44.6
|
1.0
|
|
Iron binding site 8 out
of 8 in 1zzh
Go back to
Iron Binding Sites List in 1zzh
Iron binding site 8 out
of 8 in the Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Structure of the Fully Oxidized Di-Heme Cytochrome C Peroxidase From R. Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe402
b:38.0
occ:1.00
|
FE
|
D:HEC402
|
0.0
|
38.0
|
1.0
|
NA
|
D:HEC402
|
1.9
|
36.4
|
1.0
|
NB
|
D:HEC402
|
1.9
|
35.8
|
1.0
|
ND
|
D:HEC402
|
2.0
|
36.5
|
1.0
|
NC
|
D:HEC402
|
2.0
|
40.4
|
1.0
|
NE2
|
D:HIS204
|
2.2
|
42.2
|
1.0
|
SD
|
D:MET278
|
2.4
|
46.0
|
1.0
|
C1A
|
D:HEC402
|
3.0
|
37.2
|
1.0
|
C4A
|
D:HEC402
|
3.0
|
36.9
|
1.0
|
C4B
|
D:HEC402
|
3.0
|
34.8
|
1.0
|
C4D
|
D:HEC402
|
3.0
|
38.0
|
1.0
|
C1B
|
D:HEC402
|
3.0
|
36.1
|
1.0
|
C1C
|
D:HEC402
|
3.0
|
41.5
|
1.0
|
C4C
|
D:HEC402
|
3.0
|
41.5
|
1.0
|
C1D
|
D:HEC402
|
3.0
|
39.5
|
1.0
|
CD2
|
D:HIS204
|
3.1
|
42.7
|
1.0
|
CE1
|
D:HIS204
|
3.2
|
42.7
|
1.0
|
CHA
|
D:HEC402
|
3.4
|
36.5
|
1.0
|
CHB
|
D:HEC402
|
3.4
|
36.7
|
1.0
|
CHC
|
D:HEC402
|
3.4
|
38.1
|
1.0
|
CHD
|
D:HEC402
|
3.4
|
40.3
|
1.0
|
CG
|
D:MET278
|
3.5
|
45.9
|
1.0
|
CE
|
D:MET278
|
4.0
|
50.4
|
1.0
|
CG
|
D:HIS204
|
4.2
|
43.2
|
1.0
|
ND1
|
D:HIS204
|
4.2
|
40.6
|
1.0
|
C3A
|
D:HEC402
|
4.2
|
37.0
|
1.0
|
C3B
|
D:HEC402
|
4.2
|
38.0
|
1.0
|
C2A
|
D:HEC402
|
4.2
|
37.3
|
1.0
|
C3D
|
D:HEC402
|
4.2
|
40.4
|
1.0
|
C2B
|
D:HEC402
|
4.3
|
36.5
|
1.0
|
C3C
|
D:HEC402
|
4.3
|
44.1
|
1.0
|
C2C
|
D:HEC402
|
4.3
|
43.8
|
1.0
|
C2D
|
D:HEC402
|
4.3
|
40.9
|
1.0
|
CB
|
D:MET278
|
4.6
|
42.5
|
1.0
|
|
Reference:
L.De Smet,
S.N.Savvides,
E.Van Horen,
G.Pettigrew,
J.J.Van Beeumen.
Structural and Mutagenesis Studies on the Cytochrome C Peroxidase From Rhodobacter Capsulatus Provide New Insights Into Structure-Function Relationships of Bacterial Di-Heme Peroxidases J.Biol.Chem. V. 281 4371 2006.
ISSN: ISSN 0021-9258
PubMed: 16314410
DOI: 10.1074/JBC.M509582200
Page generated: Sat Aug 3 18:45:30 2024
|