Iron in PDB 4aul: 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: 4aul
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)
|
28.96 /
1.50
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
200.958,
121.919,
124.919,
90.00,
115.28,
90.00
|
R / Rfree (%)
|
14.296 /
19.334
|
Other elements in 4aul:
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 4aul). 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, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum, PDB code: 4aul:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 4aul
Go back to
Iron Binding Sites List in 4aul
Iron binding site 1 out
of 4 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:Fe754
b:10.1
occ:1.00
|
FE
|
A:HEM754
|
0.0
|
10.1
|
1.0
|
OH
|
A:TYR369
|
1.9
|
9.8
|
1.0
|
NC
|
A:HEM754
|
2.0
|
8.9
|
1.0
|
NA
|
A:HEM754
|
2.0
|
7.6
|
1.0
|
ND
|
A:HEM754
|
2.1
|
8.4
|
1.0
|
NB
|
A:HEM754
|
2.1
|
8.6
|
1.0
|
CZ
|
A:TYR369
|
2.9
|
8.5
|
1.0
|
C4C
|
A:HEM754
|
3.0
|
8.3
|
1.0
|
C4A
|
A:HEM754
|
3.1
|
7.8
|
1.0
|
C1D
|
A:HEM754
|
3.1
|
7.9
|
1.0
|
C1C
|
A:HEM754
|
3.1
|
8.7
|
1.0
|
C4B
|
A:HEM754
|
3.1
|
8.4
|
1.0
|
C1A
|
A:HEM754
|
3.1
|
6.8
|
1.0
|
C4D
|
A:HEM754
|
3.1
|
6.7
|
1.0
|
C1B
|
A:HEM754
|
3.1
|
8.8
|
1.0
|
CHD
|
A:HEM754
|
3.5
|
8.3
|
1.0
|
CHC
|
A:HEM754
|
3.5
|
9.8
|
1.0
|
CHB
|
A:HEM754
|
3.5
|
9.0
|
1.0
|
CHA
|
A:HEM754
|
3.5
|
7.7
|
1.0
|
CE2
|
A:TYR369
|
3.6
|
8.4
|
1.0
|
O
|
A:HOH2121
|
3.7
|
15.8
|
1.0
|
CE1
|
A:TYR369
|
3.9
|
10.0
|
1.0
|
NE
|
A:ARG365
|
4.1
|
7.7
|
1.0
|
NH2
|
A:ARG365
|
4.2
|
7.5
|
1.0
|
C3A
|
A:HEM754
|
4.3
|
6.8
|
1.0
|
C3C
|
A:HEM754
|
4.3
|
7.7
|
1.0
|
C2A
|
A:HEM754
|
4.3
|
6.8
|
1.0
|
C2C
|
A:HEM754
|
4.4
|
7.9
|
1.0
|
C2D
|
A:HEM754
|
4.4
|
8.5
|
1.0
|
C3B
|
A:HEM754
|
4.4
|
8.3
|
1.0
|
C3D
|
A:HEM754
|
4.4
|
7.0
|
1.0
|
C2B
|
A:HEM754
|
4.4
|
9.1
|
1.0
|
CZ
|
A:ARG365
|
4.5
|
7.6
|
1.0
|
CG2
|
A:VAL81
|
4.6
|
7.5
|
1.0
|
CZ
|
A:PHE168
|
4.7
|
7.0
|
1.0
|
CD2
|
A:TYR369
|
4.9
|
7.8
|
1.0
|
CE2
|
A:PHE168
|
4.9
|
7.2
|
1.0
|
|
Iron binding site 2 out
of 4 in 4aul
Go back to
Iron Binding Sites List in 4aul
Iron binding site 2 out
of 4 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:Fe754
b:10.5
occ:1.00
|
FE
|
B:HEM754
|
0.0
|
10.5
|
1.0
|
NC
|
B:HEM754
|
2.0
|
9.6
|
1.0
|
NA
|
B:HEM754
|
2.0
|
9.2
|
1.0
|
OH
|
B:TYR369
|
2.0
|
9.9
|
1.0
|
ND
|
B:HEM754
|
2.1
|
8.0
|
1.0
|
NB
|
B:HEM754
|
2.1
|
9.1
|
1.0
|
CZ
|
B:TYR369
|
2.9
|
9.1
|
1.0
|
C1A
|
B:HEM754
|
3.1
|
7.9
|
1.0
|
C4D
|
B:HEM754
|
3.1
|
8.0
|
1.0
|
C4C
|
B:HEM754
|
3.1
|
9.5
|
1.0
|
C1B
|
B:HEM754
|
3.1
|
9.1
|
1.0
|
C1C
|
B:HEM754
|
3.1
|
8.7
|
1.0
|
C1D
|
B:HEM754
|
3.1
|
8.3
|
1.0
|
C4B
|
B:HEM754
|
3.1
|
9.5
|
1.0
|
C4A
|
B:HEM754
|
3.1
|
9.4
|
1.0
|
CHA
|
B:HEM754
|
3.5
|
8.4
|
1.0
|
CHB
|
B:HEM754
|
3.5
|
10.4
|
1.0
|
CHC
|
B:HEM754
|
3.5
|
11.4
|
1.0
|
CHD
|
B:HEM754
|
3.5
|
8.3
|
1.0
|
CE2
|
B:TYR369
|
3.6
|
8.1
|
1.0
|
O
|
B:HOH2112
|
3.8
|
18.6
|
1.0
|
CE1
|
B:TYR369
|
3.9
|
10.7
|
1.0
|
NE
|
B:ARG365
|
4.0
|
8.3
|
1.0
|
NH2
|
B:ARG365
|
4.1
|
8.1
|
1.0
|
C3C
|
B:HEM754
|
4.3
|
9.8
|
1.0
|
C2A
|
B:HEM754
|
4.4
|
8.9
|
1.0
|
C2C
|
B:HEM754
|
4.4
|
9.7
|
1.0
|
C3D
|
B:HEM754
|
4.4
|
7.2
|
1.0
|
C3A
|
B:HEM754
|
4.4
|
8.1
|
1.0
|
C2B
|
B:HEM754
|
4.4
|
8.1
|
1.0
|
C3B
|
B:HEM754
|
4.4
|
9.0
|
1.0
|
C2D
|
B:HEM754
|
4.4
|
9.2
|
1.0
|
CG2
|
B:VAL81
|
4.5
|
8.7
|
1.0
|
CZ
|
B:ARG365
|
4.5
|
8.3
|
1.0
|
CZ
|
B:PHE168
|
4.7
|
9.7
|
1.0
|
CD2
|
B:TYR369
|
4.8
|
8.2
|
1.0
|
CE2
|
B:PHE168
|
5.0
|
8.4
|
1.0
|
|
Iron binding site 3 out
of 4 in 4aul
Go back to
Iron Binding Sites List in 4aul
Iron binding site 3 out
of 4 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:Fe754
b:10.3
occ:1.00
|
FE
|
C:HEM754
|
0.0
|
10.3
|
1.0
|
OH
|
C:TYR369
|
2.0
|
8.6
|
1.0
|
NC
|
C:HEM754
|
2.0
|
9.0
|
1.0
|
NA
|
C:HEM754
|
2.0
|
8.0
|
1.0
|
NB
|
C:HEM754
|
2.0
|
7.9
|
1.0
|
ND
|
C:HEM754
|
2.1
|
7.9
|
1.0
|
CZ
|
C:TYR369
|
2.9
|
8.0
|
1.0
|
C1B
|
C:HEM754
|
3.1
|
8.4
|
1.0
|
C4A
|
C:HEM754
|
3.1
|
7.7
|
1.0
|
C1A
|
C:HEM754
|
3.1
|
8.3
|
1.0
|
C4C
|
C:HEM754
|
3.1
|
7.8
|
1.0
|
C4D
|
C:HEM754
|
3.1
|
7.2
|
1.0
|
C1C
|
C:HEM754
|
3.1
|
9.4
|
1.0
|
C4B
|
C:HEM754
|
3.1
|
8.9
|
1.0
|
C1D
|
C:HEM754
|
3.1
|
7.7
|
1.0
|
CHB
|
C:HEM754
|
3.4
|
8.5
|
1.0
|
CHA
|
C:HEM754
|
3.5
|
7.5
|
1.0
|
CHC
|
C:HEM754
|
3.5
|
10.9
|
1.0
|
CHD
|
C:HEM754
|
3.6
|
7.6
|
1.0
|
CE2
|
C:TYR369
|
3.6
|
8.7
|
1.0
|
O
|
C:HOH2042
|
3.8
|
16.7
|
1.0
|
CE1
|
C:TYR369
|
3.9
|
9.5
|
1.0
|
NE
|
C:ARG365
|
4.0
|
7.8
|
1.0
|
NH2
|
C:ARG365
|
4.1
|
7.5
|
1.0
|
C3A
|
C:HEM754
|
4.3
|
7.9
|
1.0
|
C3C
|
C:HEM754
|
4.3
|
7.7
|
1.0
|
C2A
|
C:HEM754
|
4.4
|
8.1
|
1.0
|
C3B
|
C:HEM754
|
4.4
|
9.3
|
1.0
|
C2B
|
C:HEM754
|
4.4
|
7.8
|
1.0
|
C3D
|
C:HEM754
|
4.4
|
7.0
|
1.0
|
C2D
|
C:HEM754
|
4.4
|
7.6
|
1.0
|
C2C
|
C:HEM754
|
4.4
|
8.8
|
1.0
|
CZ
|
C:ARG365
|
4.5
|
7.6
|
1.0
|
CG2
|
C:VAL81
|
4.6
|
6.9
|
1.0
|
CZ
|
C:PHE168
|
4.7
|
7.9
|
1.0
|
CD2
|
C:TYR369
|
4.9
|
8.0
|
1.0
|
CE2
|
C:PHE168
|
5.0
|
8.2
|
1.0
|
|
Iron binding site 4 out
of 4 in 4aul
Go back to
Iron Binding Sites List in 4aul
Iron binding site 4 out
of 4 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:Fe754
b:10.4
occ:1.00
|
FE
|
D:HEM754
|
0.0
|
10.4
|
1.0
|
NA
|
D:HEM754
|
2.0
|
9.2
|
1.0
|
NC
|
D:HEM754
|
2.0
|
8.1
|
1.0
|
OH
|
D:TYR369
|
2.0
|
11.7
|
1.0
|
NB
|
D:HEM754
|
2.1
|
9.2
|
1.0
|
ND
|
D:HEM754
|
2.1
|
7.9
|
1.0
|
CZ
|
D:TYR369
|
3.0
|
9.6
|
1.0
|
C4A
|
D:HEM754
|
3.0
|
8.6
|
1.0
|
C1A
|
D:HEM754
|
3.1
|
8.8
|
1.0
|
C1C
|
D:HEM754
|
3.1
|
9.5
|
1.0
|
C1B
|
D:HEM754
|
3.1
|
9.8
|
1.0
|
C4B
|
D:HEM754
|
3.1
|
10.2
|
1.0
|
C4C
|
D:HEM754
|
3.1
|
7.4
|
1.0
|
C4D
|
D:HEM754
|
3.1
|
8.0
|
1.0
|
C1D
|
D:HEM754
|
3.1
|
6.9
|
1.0
|
CHB
|
D:HEM754
|
3.4
|
8.9
|
1.0
|
CHC
|
D:HEM754
|
3.5
|
9.6
|
1.0
|
CHD
|
D:HEM754
|
3.5
|
7.6
|
1.0
|
CHA
|
D:HEM754
|
3.5
|
8.4
|
1.0
|
CE2
|
D:TYR369
|
3.6
|
9.5
|
1.0
|
O
|
D:HOH2036
|
3.7
|
15.4
|
1.0
|
CE1
|
D:TYR369
|
3.9
|
10.1
|
1.0
|
NE
|
D:ARG365
|
4.1
|
9.0
|
1.0
|
NH2
|
D:ARG365
|
4.2
|
8.0
|
1.0
|
C3A
|
D:HEM754
|
4.3
|
7.4
|
1.0
|
C2A
|
D:HEM754
|
4.3
|
7.3
|
1.0
|
C3C
|
D:HEM754
|
4.4
|
8.0
|
1.0
|
C3B
|
D:HEM754
|
4.4
|
11.3
|
1.0
|
C2C
|
D:HEM754
|
4.4
|
7.9
|
1.0
|
C2B
|
D:HEM754
|
4.4
|
8.2
|
1.0
|
C2D
|
D:HEM754
|
4.4
|
7.0
|
1.0
|
C3D
|
D:HEM754
|
4.4
|
7.4
|
1.0
|
CZ
|
D:ARG365
|
4.5
|
8.2
|
1.0
|
CG2
|
D:VAL81
|
4.6
|
8.7
|
1.0
|
CZ
|
D:PHE168
|
4.6
|
11.1
|
1.0
|
CD2
|
D:TYR369
|
4.9
|
9.4
|
1.0
|
CE2
|
D:PHE168
|
4.9
|
10.6
|
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 23:45:46 2024
|