Iron in PDB 6qzo: Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis
Protein crystallography data
The structure of Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis, PDB code: 6qzo
was solved by
H.J.Rozeboom,
M.W.Fraaije,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
58.87 /
2.40
|
|
Space group
|
P 62
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
173.989,
173.989,
283.003,
90.00,
90.00,
120.00
|
|
R / Rfree (%)
|
24.2 /
26.7
|
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis
(pdb code 6qzo). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the
Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis, PDB code: 6qzo:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 6qzo
Go back to
Iron Binding Sites List in 6qzo
Iron binding site 1 out
of 8 in the Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis
 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 Dyp-Type Peroxidase From Cellulomonas Bogoriensis within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe401
b:20.9
occ:1.00
|
FE
|
A:HEM401
|
0.0
|
20.9
|
1.0
|
|
ND
|
A:HEM401
|
1.9
|
21.1
|
1.0
|
|
NA
|
A:HEM401
|
2.0
|
21.2
|
1.0
|
|
NE2
|
A:HIS292
|
2.1
|
19.4
|
1.0
|
|
NC
|
A:HEM401
|
2.1
|
20.3
|
1.0
|
|
NB
|
A:HEM401
|
2.1
|
20.7
|
1.0
|
|
C4D
|
A:HEM401
|
2.9
|
21.5
|
1.0
|
|
C1D
|
A:HEM401
|
2.9
|
20.5
|
1.0
|
|
C1A
|
A:HEM401
|
3.0
|
21.5
|
1.0
|
|
C4A
|
A:HEM401
|
3.0
|
21.7
|
1.0
|
|
CD2
|
A:HIS292
|
3.1
|
20.1
|
1.0
|
|
C4B
|
A:HEM401
|
3.1
|
20.6
|
1.0
|
|
C1B
|
A:HEM401
|
3.1
|
20.6
|
1.0
|
|
C4C
|
A:HEM401
|
3.1
|
20.4
|
1.0
|
|
C1C
|
A:HEM401
|
3.1
|
20.8
|
1.0
|
|
CE1
|
A:HIS292
|
3.1
|
19.8
|
1.0
|
|
CHA
|
A:HEM401
|
3.3
|
21.5
|
1.0
|
|
CHD
|
A:HEM401
|
3.4
|
21.0
|
1.0
|
|
CHB
|
A:HEM401
|
3.5
|
20.9
|
1.0
|
|
CHC
|
A:HEM401
|
3.5
|
21.2
|
1.0
|
|
C3D
|
A:HEM401
|
4.2
|
22.1
|
1.0
|
|
C2D
|
A:HEM401
|
4.2
|
21.3
|
1.0
|
|
NH1
|
A:ARG307
|
4.2
|
15.2
|
1.0
|
|
C2A
|
A:HEM401
|
4.2
|
22.1
|
1.0
|
|
C3A
|
A:HEM401
|
4.2
|
22.4
|
1.0
|
|
CG
|
A:HIS292
|
4.2
|
20.3
|
1.0
|
|
ND1
|
A:HIS292
|
4.2
|
19.9
|
1.0
|
|
C2C
|
A:HEM401
|
4.3
|
20.5
|
1.0
|
|
C3C
|
A:HEM401
|
4.3
|
21.0
|
1.0
|
|
C2B
|
A:HEM401
|
4.3
|
21.6
|
1.0
|
|
C3B
|
A:HEM401
|
4.3
|
20.7
|
1.0
|
|
OE1
|
A:GLU201
|
4.4
|
35.8
|
1.0
|
|
CE1
|
A:PHE328
|
4.8
|
18.6
|
1.0
|
|
CZ
|
A:PHE328
|
4.9
|
18.8
|
1.0
|
|
CD
|
A:ARG307
|
4.9
|
14.9
|
1.0
|
|
OE2
|
A:GLU201
|
4.9
|
33.2
|
1.0
|
|
Iron binding site 2 out
of 8 in 6qzo
Go back to
Iron Binding Sites List in 6qzo
Iron binding site 2 out
of 8 in the Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis
 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 Dyp-Type Peroxidase From Cellulomonas Bogoriensis within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe401
b:17.9
occ:1.00
|
FE
|
B:HEM401
|
0.0
|
17.9
|
1.0
|
|
ND
|
B:HEM401
|
1.9
|
18.4
|
1.0
|
|
NA
|
B:HEM401
|
2.0
|
18.1
|
1.0
|
|
NC
|
B:HEM401
|
2.1
|
18.6
|
1.0
|
|
NB
|
B:HEM401
|
2.1
|
17.8
|
1.0
|
|
NE2
|
B:HIS292
|
2.1
|
15.7
|
1.0
|
|
C1D
|
B:HEM401
|
2.9
|
18.3
|
1.0
|
|
C4D
|
B:HEM401
|
2.9
|
17.7
|
1.0
|
|
C1A
|
B:HEM401
|
3.0
|
18.4
|
1.0
|
|
C4A
|
B:HEM401
|
3.0
|
18.3
|
1.0
|
|
CD2
|
B:HIS292
|
3.1
|
16.2
|
1.0
|
|
C4B
|
B:HEM401
|
3.1
|
17.8
|
1.0
|
|
C4C
|
B:HEM401
|
3.1
|
18.8
|
1.0
|
|
C1B
|
B:HEM401
|
3.1
|
17.6
|
1.0
|
|
C1C
|
B:HEM401
|
3.1
|
18.9
|
1.0
|
|
CE1
|
B:HIS292
|
3.2
|
15.7
|
1.0
|
|
CHA
|
B:HEM401
|
3.3
|
18.3
|
1.0
|
|
CHD
|
B:HEM401
|
3.4
|
18.6
|
1.0
|
|
CHB
|
B:HEM401
|
3.5
|
18.2
|
1.0
|
|
CHC
|
B:HEM401
|
3.5
|
18.6
|
1.0
|
|
NH1
|
B:ARG307
|
4.1
|
14.6
|
1.0
|
|
C2D
|
B:HEM401
|
4.1
|
18.5
|
1.0
|
|
C3D
|
B:HEM401
|
4.2
|
18.4
|
1.0
|
|
C2A
|
B:HEM401
|
4.2
|
18.6
|
1.0
|
|
C3A
|
B:HEM401
|
4.2
|
18.3
|
1.0
|
|
CG
|
B:HIS292
|
4.3
|
15.9
|
1.0
|
|
ND1
|
B:HIS292
|
4.3
|
15.5
|
1.0
|
|
C3C
|
B:HEM401
|
4.3
|
19.8
|
1.0
|
|
C2C
|
B:HEM401
|
4.3
|
18.9
|
1.0
|
|
C2B
|
B:HEM401
|
4.3
|
17.5
|
1.0
|
|
C3B
|
B:HEM401
|
4.4
|
17.8
|
1.0
|
|
OE1
|
B:GLU201
|
4.4
|
38.5
|
1.0
|
|
CE1
|
B:PHE328
|
4.8
|
15.7
|
1.0
|
|
CZ
|
B:PHE328
|
4.9
|
15.5
|
1.0
|
|
CD
|
B:ARG307
|
4.9
|
14.0
|
1.0
|
|
OE2
|
B:GLU201
|
4.9
|
32.6
|
1.0
|
|
Iron binding site 3 out
of 8 in 6qzo
Go back to
Iron Binding Sites List in 6qzo
Iron binding site 3 out
of 8 in the Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis
 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 Dyp-Type Peroxidase From Cellulomonas Bogoriensis within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe401
b:18.2
occ:1.00
|
FE
|
C:HEM401
|
0.0
|
18.2
|
1.0
|
|
ND
|
C:HEM401
|
1.9
|
19.3
|
1.0
|
|
NA
|
C:HEM401
|
2.0
|
18.6
|
1.0
|
|
NE2
|
C:HIS292
|
2.1
|
15.7
|
1.0
|
|
NC
|
C:HEM401
|
2.1
|
18.4
|
1.0
|
|
NB
|
C:HEM401
|
2.1
|
18.8
|
1.0
|
|
C4D
|
C:HEM401
|
2.9
|
18.4
|
1.0
|
|
C1D
|
C:HEM401
|
2.9
|
18.4
|
1.0
|
|
C1A
|
C:HEM401
|
3.0
|
18.9
|
1.0
|
|
CD2
|
C:HIS292
|
3.0
|
15.9
|
1.0
|
|
C4A
|
C:HEM401
|
3.1
|
18.4
|
1.0
|
|
C1B
|
C:HEM401
|
3.1
|
18.5
|
1.0
|
|
C4C
|
C:HEM401
|
3.1
|
18.6
|
1.0
|
|
C4B
|
C:HEM401
|
3.1
|
18.7
|
1.0
|
|
C1C
|
C:HEM401
|
3.1
|
18.9
|
1.0
|
|
CE1
|
C:HIS292
|
3.1
|
15.6
|
1.0
|
|
CHA
|
C:HEM401
|
3.3
|
19.4
|
1.0
|
|
CHD
|
C:HEM401
|
3.4
|
18.5
|
1.0
|
|
CHB
|
C:HEM401
|
3.5
|
18.4
|
1.0
|
|
CHC
|
C:HEM401
|
3.5
|
19.0
|
1.0
|
|
C2D
|
C:HEM401
|
4.2
|
18.4
|
1.0
|
|
C3D
|
C:HEM401
|
4.2
|
18.4
|
1.0
|
|
CG
|
C:HIS292
|
4.2
|
16.0
|
1.0
|
|
C2A
|
C:HEM401
|
4.2
|
18.3
|
1.0
|
|
ND1
|
C:HIS292
|
4.2
|
15.7
|
1.0
|
|
C3A
|
C:HEM401
|
4.2
|
18.2
|
1.0
|
|
C2C
|
C:HEM401
|
4.3
|
19.1
|
1.0
|
|
NH2
|
C:ARG307
|
4.3
|
13.0
|
1.0
|
|
C3C
|
C:HEM401
|
4.3
|
19.2
|
1.0
|
|
C2B
|
C:HEM401
|
4.3
|
19.2
|
1.0
|
|
C3B
|
C:HEM401
|
4.3
|
18.9
|
1.0
|
|
OE1
|
C:GLU201
|
4.4
|
30.5
|
1.0
|
|
CE1
|
C:PHE328
|
4.9
|
15.6
|
1.0
|
|
OE2
|
C:GLU201
|
4.9
|
30.1
|
1.0
|
|
CZ
|
C:PHE328
|
4.9
|
15.9
|
1.0
|
|
CD
|
C:ARG307
|
5.0
|
12.6
|
1.0
|
|
Iron binding site 4 out
of 8 in 6qzo
Go back to
Iron Binding Sites List in 6qzo
Iron binding site 4 out
of 8 in the Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis
 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 Dyp-Type Peroxidase From Cellulomonas Bogoriensis within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe401
b:25.4
occ:1.00
|
FE
|
D:HEM401
|
0.0
|
25.4
|
1.0
|
|
ND
|
D:HEM401
|
1.9
|
25.6
|
1.0
|
|
NA
|
D:HEM401
|
2.0
|
25.0
|
1.0
|
|
NC
|
D:HEM401
|
2.1
|
25.7
|
1.0
|
|
NE2
|
D:HIS292
|
2.1
|
24.4
|
1.0
|
|
NB
|
D:HEM401
|
2.1
|
25.5
|
1.0
|
|
C4D
|
D:HEM401
|
2.9
|
25.7
|
1.0
|
|
C1D
|
D:HEM401
|
2.9
|
24.8
|
1.0
|
|
C1A
|
D:HEM401
|
3.0
|
26.2
|
1.0
|
|
CD2
|
D:HIS292
|
3.0
|
24.6
|
1.0
|
|
C4A
|
D:HEM401
|
3.0
|
25.6
|
1.0
|
|
C4C
|
D:HEM401
|
3.1
|
25.9
|
1.0
|
|
C4B
|
D:HEM401
|
3.1
|
24.5
|
1.0
|
|
C1C
|
D:HEM401
|
3.1
|
25.6
|
1.0
|
|
C1B
|
D:HEM401
|
3.1
|
24.4
|
1.0
|
|
CE1
|
D:HIS292
|
3.2
|
24.5
|
1.0
|
|
CHA
|
D:HEM401
|
3.3
|
27.6
|
1.0
|
|
CHD
|
D:HEM401
|
3.4
|
25.7
|
1.0
|
|
CHB
|
D:HEM401
|
3.5
|
24.6
|
1.0
|
|
CHC
|
D:HEM401
|
3.5
|
25.6
|
1.0
|
|
C2D
|
D:HEM401
|
4.2
|
26.0
|
1.0
|
|
C3D
|
D:HEM401
|
4.2
|
26.2
|
1.0
|
|
C2A
|
D:HEM401
|
4.2
|
25.8
|
1.0
|
|
C3A
|
D:HEM401
|
4.2
|
26.1
|
1.0
|
|
CG
|
D:HIS292
|
4.2
|
24.4
|
1.0
|
|
NH2
|
D:ARG307
|
4.2
|
20.5
|
1.0
|
|
ND1
|
D:HIS292
|
4.3
|
24.2
|
1.0
|
|
C2C
|
D:HEM401
|
4.3
|
25.5
|
1.0
|
|
C3C
|
D:HEM401
|
4.3
|
26.2
|
1.0
|
|
OE1
|
D:GLU201
|
4.3
|
41.8
|
1.0
|
|
C2B
|
D:HEM401
|
4.3
|
24.3
|
1.0
|
|
C3B
|
D:HEM401
|
4.4
|
24.5
|
1.0
|
|
OE2
|
D:GLU201
|
4.9
|
39.2
|
1.0
|
|
CE1
|
D:PHE328
|
4.9
|
19.6
|
1.0
|
|
CD
|
D:ARG307
|
5.0
|
20.0
|
1.0
|
|
Iron binding site 5 out
of 8 in 6qzo
Go back to
Iron Binding Sites List in 6qzo
Iron binding site 5 out
of 8 in the Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe401
b:20.4
occ:1.00
|
FE
|
E:HEM401
|
0.0
|
20.4
|
1.0
|
|
ND
|
E:HEM401
|
1.9
|
19.5
|
1.0
|
|
NA
|
E:HEM401
|
2.0
|
19.2
|
1.0
|
|
NE2
|
E:HIS292
|
2.1
|
18.6
|
1.0
|
|
NC
|
E:HEM401
|
2.1
|
18.9
|
1.0
|
|
NB
|
E:HEM401
|
2.1
|
18.7
|
1.0
|
|
C4D
|
E:HEM401
|
2.9
|
20.1
|
1.0
|
|
C1D
|
E:HEM401
|
2.9
|
19.3
|
1.0
|
|
C1A
|
E:HEM401
|
3.0
|
19.5
|
1.0
|
|
CD2
|
E:HIS292
|
3.0
|
18.5
|
1.0
|
|
C4A
|
E:HEM401
|
3.1
|
19.5
|
1.0
|
|
C4C
|
E:HEM401
|
3.1
|
19.1
|
1.0
|
|
C4B
|
E:HEM401
|
3.1
|
18.8
|
1.0
|
|
C1B
|
E:HEM401
|
3.1
|
19.1
|
1.0
|
|
C1C
|
E:HEM401
|
3.1
|
19.0
|
1.0
|
|
CE1
|
E:HIS292
|
3.1
|
18.7
|
1.0
|
|
CHA
|
E:HEM401
|
3.3
|
20.8
|
1.0
|
|
CHD
|
E:HEM401
|
3.4
|
19.0
|
1.0
|
|
CHB
|
E:HEM401
|
3.5
|
19.3
|
1.0
|
|
CHC
|
E:HEM401
|
3.5
|
18.7
|
1.0
|
|
C2D
|
E:HEM401
|
4.1
|
19.8
|
1.0
|
|
C3D
|
E:HEM401
|
4.1
|
19.9
|
1.0
|
|
CG
|
E:HIS292
|
4.2
|
18.2
|
1.0
|
|
ND1
|
E:HIS292
|
4.2
|
18.3
|
1.0
|
|
C2A
|
E:HEM401
|
4.2
|
19.9
|
1.0
|
|
C3A
|
E:HEM401
|
4.3
|
19.9
|
1.0
|
|
NH2
|
E:ARG307
|
4.3
|
15.1
|
1.0
|
|
C2C
|
E:HEM401
|
4.3
|
18.8
|
1.0
|
|
C3C
|
E:HEM401
|
4.3
|
19.5
|
1.0
|
|
C2B
|
E:HEM401
|
4.3
|
18.7
|
1.0
|
|
C3B
|
E:HEM401
|
4.4
|
18.5
|
1.0
|
|
OE1
|
E:GLU201
|
4.4
|
30.3
|
1.0
|
|
CE1
|
E:PHE328
|
4.9
|
18.0
|
1.0
|
|
CD
|
E:ARG307
|
4.9
|
15.6
|
1.0
|
|
OE2
|
E:GLU201
|
4.9
|
29.2
|
1.0
|
|
CZ
|
E:PHE328
|
4.9
|
18.0
|
1.0
|
|
Iron binding site 6 out
of 8 in 6qzo
Go back to
Iron Binding Sites List in 6qzo
Iron binding site 6 out
of 8 in the Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe401
b:25.3
occ:1.00
|
FE
|
F:HEM401
|
0.0
|
25.3
|
1.0
|
|
ND
|
F:HEM401
|
1.9
|
25.0
|
1.0
|
|
NA
|
F:HEM401
|
2.0
|
24.3
|
1.0
|
|
NC
|
F:HEM401
|
2.1
|
23.6
|
1.0
|
|
NB
|
F:HEM401
|
2.1
|
24.6
|
1.0
|
|
NE2
|
F:HIS292
|
2.1
|
26.1
|
1.0
|
|
C1D
|
F:HEM401
|
2.9
|
25.2
|
1.0
|
|
C4D
|
F:HEM401
|
2.9
|
25.7
|
1.0
|
|
C1A
|
F:HEM401
|
3.0
|
25.7
|
1.0
|
|
C4C
|
F:HEM401
|
3.0
|
23.7
|
1.0
|
|
C4A
|
F:HEM401
|
3.0
|
25.1
|
1.0
|
|
CD2
|
F:HIS292
|
3.1
|
26.3
|
1.0
|
|
C4B
|
F:HEM401
|
3.1
|
24.5
|
1.0
|
|
C1B
|
F:HEM401
|
3.1
|
24.1
|
1.0
|
|
C1C
|
F:HEM401
|
3.1
|
23.9
|
1.0
|
|
CE1
|
F:HIS292
|
3.2
|
26.4
|
1.0
|
|
CHA
|
F:HEM401
|
3.3
|
26.4
|
1.0
|
|
CHD
|
F:HEM401
|
3.3
|
24.1
|
1.0
|
|
CHB
|
F:HEM401
|
3.5
|
24.4
|
1.0
|
|
CHC
|
F:HEM401
|
3.5
|
24.2
|
1.0
|
|
NH1
|
F:ARG307
|
4.1
|
23.5
|
1.0
|
|
C2D
|
F:HEM401
|
4.1
|
26.4
|
1.0
|
|
C3D
|
F:HEM401
|
4.1
|
26.8
|
1.0
|
|
C2A
|
F:HEM401
|
4.2
|
25.6
|
1.0
|
|
C3A
|
F:HEM401
|
4.2
|
25.2
|
1.0
|
|
CG
|
F:HIS292
|
4.2
|
26.6
|
1.0
|
|
ND1
|
F:HIS292
|
4.3
|
26.7
|
1.0
|
|
C3C
|
F:HEM401
|
4.3
|
23.6
|
1.0
|
|
C2C
|
F:HEM401
|
4.3
|
23.3
|
1.0
|
|
C2B
|
F:HEM401
|
4.3
|
24.3
|
1.0
|
|
C3B
|
F:HEM401
|
4.4
|
23.7
|
1.0
|
|
OE1
|
F:GLU201
|
4.4
|
34.5
|
1.0
|
|
CE1
|
F:PHE328
|
4.8
|
26.3
|
1.0
|
|
CD
|
F:ARG307
|
4.9
|
23.6
|
1.0
|
|
OE2
|
F:GLU201
|
4.9
|
33.2
|
1.0
|
|
CZ
|
F:PHE328
|
4.9
|
26.4
|
1.0
|
|
CZ
|
F:ARG307
|
5.0
|
23.5
|
1.0
|
|
Iron binding site 7 out
of 8 in 6qzo
Go back to
Iron Binding Sites List in 6qzo
Iron binding site 7 out
of 8 in the Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Fe401
b:26.5
occ:1.00
|
FE
|
G:HEM401
|
0.0
|
26.5
|
1.0
|
|
ND
|
G:HEM401
|
1.9
|
25.1
|
1.0
|
|
NA
|
G:HEM401
|
2.0
|
25.2
|
1.0
|
|
NE2
|
G:HIS292
|
2.1
|
33.6
|
1.0
|
|
NC
|
G:HEM401
|
2.1
|
23.8
|
1.0
|
|
NB
|
G:HEM401
|
2.1
|
24.6
|
1.0
|
|
C1D
|
G:HEM401
|
2.9
|
25.0
|
1.0
|
|
C4D
|
G:HEM401
|
2.9
|
25.9
|
1.0
|
|
C1A
|
G:HEM401
|
3.0
|
25.3
|
1.0
|
|
CD2
|
G:HIS292
|
3.0
|
33.3
|
1.0
|
|
C4A
|
G:HEM401
|
3.0
|
25.1
|
1.0
|
|
C4C
|
G:HEM401
|
3.0
|
23.9
|
1.0
|
|
C1B
|
G:HEM401
|
3.1
|
24.8
|
1.0
|
|
C4B
|
G:HEM401
|
3.1
|
24.8
|
1.0
|
|
C1C
|
G:HEM401
|
3.1
|
23.7
|
1.0
|
|
CE1
|
G:HIS292
|
3.1
|
33.7
|
1.0
|
|
CHD
|
G:HEM401
|
3.3
|
23.7
|
1.0
|
|
CHA
|
G:HEM401
|
3.3
|
26.1
|
1.0
|
|
CHB
|
G:HEM401
|
3.4
|
25.0
|
1.0
|
|
CHC
|
G:HEM401
|
3.5
|
24.1
|
1.0
|
|
NH1
|
G:ARG307
|
4.1
|
31.7
|
1.0
|
|
C2D
|
G:HEM401
|
4.1
|
26.1
|
1.0
|
|
C3D
|
G:HEM401
|
4.1
|
26.9
|
1.0
|
|
CG
|
G:HIS292
|
4.2
|
33.3
|
1.0
|
|
C2A
|
G:HEM401
|
4.2
|
25.4
|
1.0
|
|
ND1
|
G:HIS292
|
4.2
|
33.8
|
1.0
|
|
C3A
|
G:HEM401
|
4.2
|
25.0
|
1.0
|
|
C3C
|
G:HEM401
|
4.3
|
24.9
|
1.0
|
|
C2C
|
G:HEM401
|
4.3
|
23.4
|
1.0
|
|
C2B
|
G:HEM401
|
4.3
|
24.6
|
1.0
|
|
C3B
|
G:HEM401
|
4.4
|
23.8
|
1.0
|
|
OE1
|
G:GLU201
|
4.5
|
31.6
|
1.0
|
|
OE2
|
G:GLU201
|
4.9
|
31.9
|
1.0
|
|
CD
|
G:ARG307
|
4.9
|
30.7
|
1.0
|
|
CE1
|
G:PHE328
|
4.9
|
25.6
|
1.0
|
|
CZ
|
G:ARG307
|
4.9
|
32.0
|
1.0
|
|
CZ
|
G:PHE328
|
5.0
|
25.7
|
1.0
|
|
Iron binding site 8 out
of 8 in 6qzo
Go back to
Iron Binding Sites List in 6qzo
Iron binding site 8 out
of 8 in the Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Crystal Structure of Dyp-Type Peroxidase From Cellulomonas Bogoriensis within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Fe401
b:16.6
occ:1.00
|
FE
|
H:HEM401
|
0.0
|
16.6
|
1.0
|
|
ND
|
H:HEM401
|
1.9
|
16.6
|
1.0
|
|
NA
|
H:HEM401
|
2.0
|
15.9
|
1.0
|
|
NC
|
H:HEM401
|
2.1
|
16.2
|
1.0
|
|
NE2
|
H:HIS292
|
2.1
|
18.9
|
1.0
|
|
NB
|
H:HEM401
|
2.1
|
16.3
|
1.0
|
|
C1D
|
H:HEM401
|
2.9
|
16.6
|
1.0
|
|
C4D
|
H:HEM401
|
2.9
|
16.9
|
1.0
|
|
C1A
|
H:HEM401
|
3.0
|
16.3
|
1.0
|
|
CD2
|
H:HIS292
|
3.0
|
19.1
|
1.0
|
|
C4A
|
H:HEM401
|
3.0
|
15.8
|
1.0
|
|
C4C
|
H:HEM401
|
3.0
|
16.1
|
1.0
|
|
C1B
|
H:HEM401
|
3.1
|
16.1
|
1.0
|
|
C4B
|
H:HEM401
|
3.1
|
16.4
|
1.0
|
|
C1C
|
H:HEM401
|
3.1
|
16.4
|
1.0
|
|
CE1
|
H:HIS292
|
3.2
|
19.4
|
1.0
|
|
CHD
|
H:HEM401
|
3.4
|
16.1
|
1.0
|
|
CHA
|
H:HEM401
|
3.4
|
16.8
|
1.0
|
|
CHB
|
H:HEM401
|
3.4
|
15.9
|
1.0
|
|
CHC
|
H:HEM401
|
3.5
|
16.3
|
1.0
|
|
NH2
|
H:ARG307
|
4.2
|
18.5
|
1.0
|
|
C2D
|
H:HEM401
|
4.2
|
17.4
|
1.0
|
|
C3A
|
H:HEM401
|
4.2
|
16.0
|
1.0
|
|
C2A
|
H:HEM401
|
4.2
|
16.3
|
1.0
|
|
CG
|
H:HIS292
|
4.2
|
19.3
|
1.0
|
|
C3D
|
H:HEM401
|
4.2
|
17.4
|
1.0
|
|
ND1
|
H:HIS292
|
4.2
|
19.2
|
1.0
|
|
C3C
|
H:HEM401
|
4.3
|
15.9
|
1.0
|
|
C2C
|
H:HEM401
|
4.3
|
16.1
|
1.0
|
|
OE1
|
H:GLU201
|
4.3
|
27.1
|
1.0
|
|
C2B
|
H:HEM401
|
4.3
|
16.2
|
1.0
|
|
C3B
|
H:HEM401
|
4.4
|
16.2
|
1.0
|
|
CE1
|
H:PHE328
|
4.9
|
15.8
|
1.0
|
|
OE2
|
H:GLU201
|
4.9
|
26.4
|
1.0
|
|
CD
|
H:ARG307
|
4.9
|
18.2
|
1.0
|
|
CZ
|
H:ARG307
|
5.0
|
18.2
|
1.0
|
|
CZ
|
H:PHE328
|
5.0
|
15.8
|
1.0
|
|
CD
|
H:GLU201
|
5.0
|
25.6
|
1.0
|
|
Reference:
M.H.Habib,
H.J.Rozeboom,
M.W.Fraaije.
Characterization of A New Dyp-Peroxidase From the Alkaliphilic Cellulomonad, Cellulomonas Bogoriensis. Molecules V. 24 2019.
ISSN: ESSN 1420-3049
PubMed: 30934796
DOI: 10.3390/MOLECULES24071208
Page generated: Sun Dec 13 16:58:21 2020
|
