Iron in PDB 4aun: Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
Enzymatic activity of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
All present enzymatic activity of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum:
1.11.1.6;
Protein crystallography data
The structure of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum, PDB code: 4aun
was solved by
Y.Yuzugullu,
C.H.Trinh,
M.A.Smith,
A.R.Pearson,
S.E.V.Phillips,
D.Sutay Kocabas,
U.Bakir,
Z.B.Ogel,
M.J.Mcpherson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
69.94 /
1.92
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
253.370,
243.290,
97.060,
90.00,
104.16,
90.00
|
R / Rfree (%)
|
16.422 /
20.054
|
Other elements in 4aun:
The structure of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
(pdb code 4aun). 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, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum, PDB code: 4aun:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 4aun
Go back to
Iron Binding Sites List in 4aun
Iron binding site 1 out
of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe900
b:16.1
occ:1.00
|
FE
|
A:HDD900
|
0.0
|
16.1
|
1.0
|
ND
|
A:HDD900
|
1.9
|
15.0
|
1.0
|
OH
|
A:TYR369
|
2.0
|
11.0
|
1.0
|
NA
|
A:HDD900
|
2.1
|
13.0
|
1.0
|
NC
|
A:HDD900
|
2.1
|
13.3
|
1.0
|
NB
|
A:HDD900
|
2.1
|
14.1
|
1.0
|
O
|
A:HOH2085
|
2.3
|
16.1
|
0.3
|
C4D
|
A:HDD900
|
2.9
|
16.6
|
1.0
|
C1D
|
A:HDD900
|
2.9
|
15.5
|
1.0
|
CZ
|
A:TYR369
|
3.0
|
10.0
|
1.0
|
C1A
|
A:HDD900
|
3.1
|
13.4
|
1.0
|
C4C
|
A:HDD900
|
3.1
|
13.7
|
1.0
|
C4A
|
A:HDD900
|
3.1
|
12.4
|
1.0
|
C1C
|
A:HDD900
|
3.1
|
12.7
|
1.0
|
C4B
|
A:HDD900
|
3.1
|
13.5
|
1.0
|
C1B
|
A:HDD900
|
3.1
|
13.5
|
1.0
|
CHA
|
A:HDD900
|
3.3
|
14.0
|
1.0
|
CHD
|
A:HDD900
|
3.3
|
13.1
|
1.0
|
CHB
|
A:HDD900
|
3.5
|
11.6
|
1.0
|
CHC
|
A:HDD900
|
3.5
|
12.1
|
1.0
|
CE1
|
A:TYR369
|
3.8
|
10.9
|
1.0
|
CE2
|
A:TYR369
|
3.9
|
10.5
|
1.0
|
NE
|
A:ARG365
|
4.2
|
10.5
|
1.0
|
NH2
|
A:ARG365
|
4.2
|
11.0
|
1.0
|
C3D
|
A:HDD900
|
4.2
|
19.5
|
1.0
|
C2D
|
A:HDD900
|
4.3
|
19.2
|
1.0
|
C3C
|
A:HDD900
|
4.4
|
12.1
|
1.0
|
O
|
A:HOH2086
|
4.4
|
25.2
|
1.0
|
C2A
|
A:HDD900
|
4.4
|
11.2
|
1.0
|
C3A
|
A:HDD900
|
4.4
|
11.2
|
1.0
|
CG2
|
A:VAL81
|
4.4
|
11.2
|
1.0
|
C3B
|
A:HDD900
|
4.4
|
13.8
|
1.0
|
C2C
|
A:HDD900
|
4.4
|
13.1
|
1.0
|
C2B
|
A:HDD900
|
4.5
|
12.4
|
1.0
|
CZ
|
A:PHE168
|
4.5
|
9.4
|
1.0
|
CZ
|
A:ARG365
|
4.6
|
11.6
|
1.0
|
CE1
|
A:HIS82
|
4.7
|
10.3
|
1.0
|
ND1
|
A:HIS82
|
4.8
|
11.5
|
1.0
|
O1D
|
A:HDD900
|
5.0
|
24.2
|
1.0
|
|
Iron binding site 2 out
of 8 in 4aun
Go back to
Iron Binding Sites List in 4aun
Iron binding site 2 out
of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe900
b:16.9
occ:1.00
|
FE
|
B:HDD900
|
0.0
|
16.9
|
1.0
|
OH
|
B:TYR369
|
1.9
|
10.2
|
1.0
|
ND
|
B:HDD900
|
1.9
|
15.0
|
1.0
|
NA
|
B:HDD900
|
2.1
|
13.8
|
1.0
|
NB
|
B:HDD900
|
2.1
|
15.2
|
1.0
|
NC
|
B:HDD900
|
2.1
|
13.5
|
1.0
|
O
|
B:HOH2057
|
2.3
|
11.1
|
0.3
|
C4D
|
B:HDD900
|
2.9
|
15.7
|
1.0
|
C1D
|
B:HDD900
|
3.0
|
16.8
|
1.0
|
CZ
|
B:TYR369
|
3.0
|
10.1
|
1.0
|
C4C
|
B:HDD900
|
3.1
|
14.6
|
1.0
|
C1A
|
B:HDD900
|
3.1
|
13.3
|
1.0
|
C4A
|
B:HDD900
|
3.1
|
12.9
|
1.0
|
C1C
|
B:HDD900
|
3.1
|
14.2
|
1.0
|
C4B
|
B:HDD900
|
3.1
|
14.8
|
1.0
|
C1B
|
B:HDD900
|
3.1
|
14.3
|
1.0
|
CHA
|
B:HDD900
|
3.3
|
14.4
|
1.0
|
CHD
|
B:HDD900
|
3.4
|
14.2
|
1.0
|
CHB
|
B:HDD900
|
3.5
|
12.7
|
1.0
|
CHC
|
B:HDD900
|
3.5
|
13.6
|
1.0
|
CE1
|
B:TYR369
|
3.8
|
10.5
|
1.0
|
CE2
|
B:TYR369
|
3.8
|
10.5
|
1.0
|
NE
|
B:ARG365
|
4.2
|
13.2
|
1.0
|
C3D
|
B:HDD900
|
4.3
|
17.2
|
1.0
|
C2D
|
B:HDD900
|
4.3
|
18.1
|
1.0
|
NH2
|
B:ARG365
|
4.3
|
12.9
|
1.0
|
C3C
|
B:HDD900
|
4.4
|
14.2
|
1.0
|
C2A
|
B:HDD900
|
4.4
|
12.2
|
1.0
|
C3B
|
B:HDD900
|
4.4
|
14.3
|
1.0
|
C3A
|
B:HDD900
|
4.4
|
12.4
|
1.0
|
C2C
|
B:HDD900
|
4.4
|
14.4
|
1.0
|
CG2
|
B:VAL81
|
4.4
|
9.9
|
1.0
|
C2B
|
B:HDD900
|
4.4
|
14.5
|
1.0
|
O
|
B:HOH2058
|
4.5
|
20.4
|
1.0
|
CZ
|
B:ARG365
|
4.7
|
13.5
|
1.0
|
CZ
|
B:PHE168
|
4.7
|
10.8
|
1.0
|
CE1
|
B:HIS82
|
4.7
|
10.3
|
1.0
|
ND1
|
B:HIS82
|
4.8
|
12.1
|
1.0
|
|
Iron binding site 3 out
of 8 in 4aun
Go back to
Iron Binding Sites List in 4aun
Iron binding site 3 out
of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe900
b:15.9
occ:1.00
|
FE
|
C:HDD900
|
0.0
|
15.9
|
1.0
|
OH
|
C:TYR369
|
1.9
|
8.3
|
1.0
|
ND
|
C:HDD900
|
1.9
|
14.5
|
1.0
|
NA
|
C:HDD900
|
2.1
|
12.7
|
1.0
|
NC
|
C:HDD900
|
2.1
|
13.3
|
1.0
|
NB
|
C:HDD900
|
2.1
|
15.0
|
1.0
|
O
|
C:HOH2469
|
2.3
|
10.1
|
0.4
|
C4D
|
C:HDD900
|
2.9
|
14.9
|
1.0
|
C1D
|
C:HDD900
|
2.9
|
15.4
|
1.0
|
CZ
|
C:TYR369
|
3.0
|
9.2
|
1.0
|
C1A
|
C:HDD900
|
3.0
|
11.7
|
1.0
|
C4C
|
C:HDD900
|
3.1
|
14.1
|
1.0
|
C4A
|
C:HDD900
|
3.1
|
12.1
|
1.0
|
C1C
|
C:HDD900
|
3.1
|
13.4
|
1.0
|
C4B
|
C:HDD900
|
3.1
|
14.4
|
1.0
|
C1B
|
C:HDD900
|
3.1
|
14.1
|
1.0
|
CHA
|
C:HDD900
|
3.3
|
12.6
|
1.0
|
CHD
|
C:HDD900
|
3.4
|
14.0
|
1.0
|
CHC
|
C:HDD900
|
3.5
|
14.0
|
1.0
|
CHB
|
C:HDD900
|
3.5
|
12.2
|
1.0
|
CE2
|
C:TYR369
|
3.7
|
8.6
|
1.0
|
CE1
|
C:TYR369
|
3.8
|
8.4
|
1.0
|
NE
|
C:ARG365
|
4.1
|
10.4
|
1.0
|
NH2
|
C:ARG365
|
4.2
|
9.3
|
1.0
|
C3D
|
C:HDD900
|
4.3
|
16.1
|
1.0
|
C2D
|
C:HDD900
|
4.3
|
17.2
|
1.0
|
O
|
C:HOH2075
|
4.3
|
17.9
|
1.0
|
C3C
|
C:HDD900
|
4.4
|
14.0
|
1.0
|
C2A
|
C:HDD900
|
4.4
|
10.4
|
1.0
|
C3A
|
C:HDD900
|
4.4
|
10.8
|
1.0
|
C3B
|
C:HDD900
|
4.4
|
14.9
|
1.0
|
C2C
|
C:HDD900
|
4.4
|
13.8
|
1.0
|
C2B
|
C:HDD900
|
4.5
|
13.8
|
1.0
|
CG2
|
C:VAL81
|
4.5
|
10.4
|
1.0
|
CZ
|
C:ARG365
|
4.6
|
9.8
|
1.0
|
CZ
|
C:PHE168
|
4.6
|
10.8
|
1.0
|
CE1
|
C:HIS82
|
4.8
|
9.6
|
1.0
|
ND1
|
C:HIS82
|
4.9
|
9.2
|
1.0
|
O1D
|
C:HDD900
|
5.0
|
18.2
|
1.0
|
CD2
|
C:TYR369
|
5.0
|
9.1
|
1.0
|
|
Iron binding site 4 out
of 8 in 4aun
Go back to
Iron Binding Sites List in 4aun
Iron binding site 4 out
of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe900
b:15.2
occ:1.00
|
FE
|
D:HDD900
|
0.0
|
15.2
|
1.0
|
ND
|
D:HDD900
|
1.9
|
13.2
|
1.0
|
OH
|
D:TYR369
|
2.0
|
9.4
|
1.0
|
NC
|
D:HDD900
|
2.1
|
11.4
|
1.0
|
NA
|
D:HDD900
|
2.1
|
11.3
|
1.0
|
NB
|
D:HDD900
|
2.1
|
11.8
|
1.0
|
O
|
D:HOH2079
|
2.5
|
7.5
|
0.3
|
C4D
|
D:HDD900
|
2.9
|
13.4
|
1.0
|
C1D
|
D:HDD900
|
2.9
|
14.3
|
1.0
|
CZ
|
D:TYR369
|
3.0
|
9.3
|
1.0
|
C4C
|
D:HDD900
|
3.0
|
11.9
|
1.0
|
C1A
|
D:HDD900
|
3.1
|
11.4
|
1.0
|
C1C
|
D:HDD900
|
3.1
|
11.0
|
1.0
|
C4B
|
D:HDD900
|
3.1
|
11.3
|
1.0
|
C4A
|
D:HDD900
|
3.1
|
10.8
|
1.0
|
C1B
|
D:HDD900
|
3.1
|
11.1
|
1.0
|
CHA
|
D:HDD900
|
3.3
|
12.2
|
1.0
|
CHD
|
D:HDD900
|
3.4
|
12.3
|
1.0
|
CHC
|
D:HDD900
|
3.4
|
10.3
|
1.0
|
CHB
|
D:HDD900
|
3.4
|
10.5
|
1.0
|
CE1
|
D:TYR369
|
3.8
|
9.0
|
1.0
|
CE2
|
D:TYR369
|
3.8
|
9.8
|
1.0
|
NE
|
D:ARG365
|
4.2
|
9.0
|
1.0
|
C3D
|
D:HDD900
|
4.3
|
16.3
|
1.0
|
C2D
|
D:HDD900
|
4.3
|
16.4
|
1.0
|
NH2
|
D:ARG365
|
4.3
|
9.6
|
1.0
|
C3C
|
D:HDD900
|
4.4
|
11.7
|
1.0
|
C3B
|
D:HDD900
|
4.4
|
11.3
|
1.0
|
C2A
|
D:HDD900
|
4.4
|
10.1
|
1.0
|
C3A
|
D:HDD900
|
4.4
|
10.4
|
1.0
|
C2C
|
D:HDD900
|
4.4
|
10.8
|
1.0
|
C2B
|
D:HDD900
|
4.4
|
10.8
|
1.0
|
CG2
|
D:VAL81
|
4.5
|
7.8
|
1.0
|
CZ
|
D:PHE168
|
4.5
|
9.3
|
1.0
|
O
|
D:HOH2080
|
4.6
|
14.7
|
1.0
|
CZ
|
D:ARG365
|
4.7
|
9.3
|
1.0
|
CE1
|
D:HIS82
|
4.7
|
8.7
|
1.0
|
ND1
|
D:HIS82
|
4.8
|
9.3
|
1.0
|
O1D
|
D:HDD900
|
5.0
|
18.3
|
1.0
|
|
Iron binding site 5 out
of 8 in 4aun
Go back to
Iron Binding Sites List in 4aun
Iron binding site 5 out
of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe900
b:16.0
occ:1.00
|
FE
|
E:HDD900
|
0.0
|
16.0
|
1.0
|
ND
|
E:HDD900
|
1.9
|
15.2
|
1.0
|
OH
|
E:TYR369
|
2.0
|
12.0
|
1.0
|
NA
|
E:HDD900
|
2.1
|
12.7
|
1.0
|
NC
|
E:HDD900
|
2.1
|
14.3
|
1.0
|
NB
|
E:HDD900
|
2.1
|
14.3
|
1.0
|
O
|
E:HOH2038
|
2.5
|
10.4
|
0.3
|
C4D
|
E:HDD900
|
2.9
|
15.0
|
1.0
|
C1D
|
E:HDD900
|
2.9
|
15.8
|
1.0
|
CZ
|
E:TYR369
|
3.0
|
11.3
|
1.0
|
C1A
|
E:HDD900
|
3.1
|
12.7
|
1.0
|
C4C
|
E:HDD900
|
3.1
|
14.2
|
1.0
|
C4A
|
E:HDD900
|
3.1
|
12.0
|
1.0
|
C4B
|
E:HDD900
|
3.1
|
13.9
|
1.0
|
C1B
|
E:HDD900
|
3.1
|
14.1
|
1.0
|
C1C
|
E:HDD900
|
3.1
|
14.0
|
1.0
|
CHA
|
E:HDD900
|
3.3
|
13.7
|
1.0
|
CHD
|
E:HDD900
|
3.4
|
15.1
|
1.0
|
CHB
|
E:HDD900
|
3.4
|
12.5
|
1.0
|
CHC
|
E:HDD900
|
3.5
|
13.7
|
1.0
|
CE2
|
E:TYR369
|
3.7
|
11.2
|
1.0
|
CE1
|
E:TYR369
|
3.8
|
11.8
|
1.0
|
NE
|
E:ARG365
|
4.2
|
12.6
|
1.0
|
NH2
|
E:ARG365
|
4.2
|
13.9
|
1.0
|
C3D
|
E:HDD900
|
4.3
|
19.5
|
1.0
|
C2D
|
E:HDD900
|
4.3
|
19.7
|
1.0
|
C2A
|
E:HDD900
|
4.4
|
11.7
|
1.0
|
C3C
|
E:HDD900
|
4.4
|
13.5
|
1.0
|
C3A
|
E:HDD900
|
4.4
|
11.0
|
1.0
|
CG2
|
E:VAL81
|
4.4
|
10.7
|
1.0
|
C3B
|
E:HDD900
|
4.4
|
14.2
|
1.0
|
C2B
|
E:HDD900
|
4.5
|
13.6
|
1.0
|
C2C
|
E:HDD900
|
4.5
|
14.0
|
1.0
|
O
|
E:HOH2039
|
4.5
|
23.2
|
1.0
|
CZ
|
E:PHE168
|
4.5
|
11.4
|
1.0
|
CZ
|
E:ARG365
|
4.6
|
14.7
|
1.0
|
CE1
|
E:HIS82
|
4.7
|
11.9
|
1.0
|
ND1
|
E:HIS82
|
4.7
|
14.2
|
1.0
|
CD2
|
E:TYR369
|
5.0
|
11.2
|
1.0
|
|
Iron binding site 6 out
of 8 in 4aun
Go back to
Iron Binding Sites List in 4aun
Iron binding site 6 out
of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe900
b:15.1
occ:1.00
|
FE
|
F:HDD900
|
0.0
|
15.1
|
1.0
|
ND
|
F:HDD900
|
1.9
|
14.4
|
1.0
|
OH
|
F:TYR369
|
2.0
|
9.8
|
1.0
|
NA
|
F:HDD900
|
2.1
|
11.7
|
1.0
|
NC
|
F:HDD900
|
2.1
|
12.3
|
1.0
|
NB
|
F:HDD900
|
2.1
|
13.1
|
1.0
|
O
|
F:HOH2380
|
2.5
|
10.0
|
0.4
|
C4D
|
F:HDD900
|
2.9
|
13.6
|
1.0
|
C1D
|
F:HDD900
|
3.0
|
14.8
|
1.0
|
CZ
|
F:TYR369
|
3.0
|
9.8
|
1.0
|
C4C
|
F:HDD900
|
3.0
|
12.7
|
1.0
|
C1A
|
F:HDD900
|
3.1
|
11.6
|
1.0
|
C4A
|
F:HDD900
|
3.1
|
10.6
|
1.0
|
C4B
|
F:HDD900
|
3.1
|
12.2
|
1.0
|
C1C
|
F:HDD900
|
3.1
|
11.5
|
1.0
|
C1B
|
F:HDD900
|
3.1
|
12.0
|
1.0
|
CHA
|
F:HDD900
|
3.3
|
13.0
|
1.0
|
CHD
|
F:HDD900
|
3.4
|
13.0
|
1.0
|
CHB
|
F:HDD900
|
3.5
|
10.7
|
1.0
|
CHC
|
F:HDD900
|
3.5
|
11.3
|
1.0
|
CE1
|
F:TYR369
|
3.8
|
9.8
|
1.0
|
CE2
|
F:TYR369
|
3.8
|
10.1
|
1.0
|
NE
|
F:ARG365
|
4.2
|
10.8
|
1.0
|
NH2
|
F:ARG365
|
4.2
|
11.3
|
1.0
|
O
|
F:HOH2052
|
4.2
|
28.3
|
1.0
|
C3D
|
F:HDD900
|
4.3
|
15.7
|
1.0
|
C2D
|
F:HDD900
|
4.3
|
16.5
|
1.0
|
C3C
|
F:HDD900
|
4.4
|
12.1
|
1.0
|
C2A
|
F:HDD900
|
4.4
|
10.8
|
1.0
|
C3B
|
F:HDD900
|
4.4
|
11.9
|
1.0
|
C3A
|
F:HDD900
|
4.4
|
10.5
|
1.0
|
CG2
|
F:VAL81
|
4.4
|
9.1
|
1.0
|
C2C
|
F:HDD900
|
4.4
|
11.9
|
1.0
|
C2B
|
F:HDD900
|
4.5
|
12.0
|
1.0
|
CE1
|
F:HIS82
|
4.6
|
8.6
|
1.0
|
CZ
|
F:PHE168
|
4.6
|
7.7
|
1.0
|
CZ
|
F:ARG365
|
4.6
|
12.4
|
1.0
|
ND1
|
F:HIS82
|
4.7
|
9.0
|
1.0
|
|
Iron binding site 7 out
of 8 in 4aun
Go back to
Iron Binding Sites List in 4aun
Iron binding site 7 out
of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Fe900
b:16.6
occ:1.00
|
FE
|
G:HDD900
|
0.0
|
16.6
|
1.0
|
OH
|
G:TYR369
|
1.9
|
11.5
|
1.0
|
ND
|
G:HDD900
|
1.9
|
14.7
|
1.0
|
NA
|
G:HDD900
|
2.1
|
13.2
|
1.0
|
NC
|
G:HDD900
|
2.1
|
14.0
|
1.0
|
NB
|
G:HDD900
|
2.1
|
14.0
|
1.0
|
O
|
G:HOH2057
|
2.5
|
8.7
|
0.3
|
C4D
|
G:HDD900
|
2.9
|
14.9
|
1.0
|
C1D
|
G:HDD900
|
2.9
|
15.6
|
1.0
|
CZ
|
G:TYR369
|
3.0
|
11.0
|
1.0
|
C1A
|
G:HDD900
|
3.1
|
13.1
|
1.0
|
C4C
|
G:HDD900
|
3.1
|
14.3
|
1.0
|
C4A
|
G:HDD900
|
3.1
|
12.6
|
1.0
|
C1C
|
G:HDD900
|
3.1
|
14.3
|
1.0
|
C4B
|
G:HDD900
|
3.1
|
14.4
|
1.0
|
C1B
|
G:HDD900
|
3.1
|
13.6
|
1.0
|
CHA
|
G:HDD900
|
3.3
|
13.9
|
1.0
|
CHD
|
G:HDD900
|
3.3
|
14.0
|
1.0
|
CHB
|
G:HDD900
|
3.4
|
12.1
|
1.0
|
CHC
|
G:HDD900
|
3.5
|
13.6
|
1.0
|
CE1
|
G:TYR369
|
3.8
|
11.4
|
1.0
|
CE2
|
G:TYR369
|
3.8
|
11.7
|
1.0
|
NE
|
G:ARG365
|
4.2
|
12.5
|
1.0
|
NH2
|
G:ARG365
|
4.2
|
12.4
|
1.0
|
C3D
|
G:HDD900
|
4.3
|
16.3
|
1.0
|
C2D
|
G:HDD900
|
4.3
|
17.4
|
1.0
|
C3C
|
G:HDD900
|
4.4
|
14.9
|
1.0
|
C2A
|
G:HDD900
|
4.4
|
11.3
|
1.0
|
C3A
|
G:HDD900
|
4.4
|
11.6
|
1.0
|
C3B
|
G:HDD900
|
4.4
|
13.9
|
1.0
|
O
|
G:HOH2058
|
4.4
|
15.2
|
1.0
|
C2C
|
G:HDD900
|
4.4
|
14.7
|
1.0
|
CG2
|
G:VAL81
|
4.5
|
10.2
|
1.0
|
C2B
|
G:HDD900
|
4.5
|
12.8
|
1.0
|
CZ
|
G:PHE168
|
4.6
|
13.9
|
1.0
|
CZ
|
G:ARG365
|
4.6
|
13.2
|
1.0
|
CE1
|
G:HIS82
|
4.6
|
12.0
|
1.0
|
ND1
|
G:HIS82
|
4.8
|
13.5
|
1.0
|
O1D
|
G:HDD900
|
5.0
|
19.1
|
1.0
|
|
Iron binding site 8 out
of 8 in 4aun
Go back to
Iron Binding Sites List in 4aun
Iron binding site 8 out
of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Fe900
b:16.5
occ:1.00
|
FE
|
H:HDD900
|
0.0
|
16.5
|
1.0
|
ND
|
H:HDD900
|
1.9
|
13.7
|
1.0
|
OH
|
H:TYR369
|
2.0
|
11.3
|
1.0
|
NA
|
H:HDD900
|
2.1
|
12.2
|
1.0
|
NB
|
H:HDD900
|
2.1
|
13.7
|
1.0
|
NC
|
H:HDD900
|
2.1
|
12.9
|
1.0
|
O
|
H:HOH2349
|
2.6
|
11.7
|
0.3
|
C4D
|
H:HDD900
|
2.9
|
16.0
|
1.0
|
C1D
|
H:HDD900
|
2.9
|
15.6
|
1.0
|
CZ
|
H:TYR369
|
3.0
|
10.3
|
1.0
|
C4C
|
H:HDD900
|
3.1
|
13.2
|
1.0
|
C1A
|
H:HDD900
|
3.1
|
12.4
|
1.0
|
C4B
|
H:HDD900
|
3.1
|
13.0
|
1.0
|
C4A
|
H:HDD900
|
3.1
|
11.4
|
1.0
|
C1C
|
H:HDD900
|
3.1
|
12.8
|
1.0
|
C1B
|
H:HDD900
|
3.1
|
12.7
|
1.0
|
CHA
|
H:HDD900
|
3.3
|
13.6
|
1.0
|
CHD
|
H:HDD900
|
3.4
|
13.1
|
1.0
|
CHB
|
H:HDD900
|
3.4
|
11.4
|
1.0
|
CHC
|
H:HDD900
|
3.5
|
13.1
|
1.0
|
CE2
|
H:TYR369
|
3.8
|
10.4
|
1.0
|
CE1
|
H:TYR369
|
3.8
|
10.7
|
1.0
|
NE
|
H:ARG365
|
4.1
|
10.9
|
1.0
|
NH2
|
H:ARG365
|
4.2
|
10.8
|
1.0
|
C3D
|
H:HDD900
|
4.2
|
19.2
|
1.0
|
C2D
|
H:HDD900
|
4.3
|
18.8
|
1.0
|
O
|
H:HOH2030
|
4.4
|
25.3
|
1.0
|
C3C
|
H:HDD900
|
4.4
|
12.7
|
1.0
|
C2A
|
H:HDD900
|
4.4
|
10.8
|
1.0
|
C3B
|
H:HDD900
|
4.4
|
13.6
|
1.0
|
C3A
|
H:HDD900
|
4.4
|
10.4
|
1.0
|
C2B
|
H:HDD900
|
4.4
|
12.9
|
1.0
|
C2C
|
H:HDD900
|
4.4
|
13.0
|
1.0
|
CG2
|
H:VAL81
|
4.5
|
8.7
|
1.0
|
CZ
|
H:ARG365
|
4.6
|
10.8
|
1.0
|
CZ
|
H:PHE168
|
4.6
|
12.7
|
1.0
|
CE1
|
H:HIS82
|
4.7
|
9.4
|
1.0
|
ND1
|
H:HIS82
|
4.7
|
10.5
|
1.0
|
O1D
|
H:HDD900
|
5.0
|
23.5
|
1.0
|
CD2
|
H:TYR369
|
5.0
|
9.6
|
1.0
|
|
Reference:
Y.Yuzugullu,
C.H.Trinh,
M.A.Smith,
A.R.Pearson,
S.E.V.Phillips,
D.Sutay Kocabas,
U.Bakir,
Z.B.Ogel,
M.J.Mcpherson.
Structure, Recombinant Expression and Mutagenesis Studies of the Catalase with Oxidase Activity From Scytalidium Thermophilum Acta Crystallogr.,Sect.D V. 69 398 2013.
ISSN: ISSN 0907-4449
PubMed: 23519415
DOI: 10.1107/S0907444912049001
Page generated: Sun Aug 4 23:45:52 2024
|