Iron in PDB 6hqw: Cytochrome P450-153 From Novosphingobium Aromaticivorans
Protein crystallography data
The structure of Cytochrome P450-153 From Novosphingobium Aromaticivorans, PDB code: 6hqw
was solved by
F.Fiorentini,
A.Mattevi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
97.98 /
2.90
|
Space group
|
P 32
|
Cell size a, b, c (Å), α, β, γ (°)
|
113.133,
113.133,
72.970,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
24.8 /
29.9
|
Iron Binding Sites:
The binding sites of Iron atom in the Cytochrome P450-153 From Novosphingobium Aromaticivorans
(pdb code 6hqw). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Cytochrome P450-153 From Novosphingobium Aromaticivorans, PDB code: 6hqw:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 6hqw
Go back to
Iron Binding Sites List in 6hqw
Iron binding site 1 out
of 2 in the Cytochrome P450-153 From Novosphingobium Aromaticivorans
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Cytochrome P450-153 From Novosphingobium Aromaticivorans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe500
b:45.0
occ:1.00
|
FE
|
A:HEM500
|
0.0
|
45.0
|
1.0
|
ND
|
A:HEM500
|
1.9
|
44.7
|
1.0
|
NA
|
A:HEM500
|
2.0
|
41.8
|
1.0
|
NB
|
A:HEM500
|
2.1
|
43.9
|
1.0
|
NC
|
A:HEM500
|
2.1
|
43.6
|
1.0
|
SG
|
A:CYS394
|
2.4
|
35.9
|
1.0
|
C1D
|
A:HEM500
|
2.9
|
42.8
|
1.0
|
C4D
|
A:HEM500
|
2.9
|
40.5
|
1.0
|
C1A
|
A:HEM500
|
2.9
|
38.3
|
1.0
|
C4A
|
A:HEM500
|
3.0
|
44.7
|
1.0
|
C1B
|
A:HEM500
|
3.0
|
44.2
|
1.0
|
C4B
|
A:HEM500
|
3.0
|
45.9
|
1.0
|
C4C
|
A:HEM500
|
3.0
|
43.9
|
1.0
|
C1C
|
A:HEM500
|
3.1
|
45.9
|
1.0
|
CHA
|
A:HEM500
|
3.3
|
39.1
|
1.0
|
CHD
|
A:HEM500
|
3.3
|
44.1
|
1.0
|
CHB
|
A:HEM500
|
3.4
|
44.8
|
1.0
|
CHC
|
A:HEM500
|
3.5
|
45.7
|
1.0
|
CB
|
A:CYS394
|
3.6
|
36.9
|
1.0
|
C2A
|
A:HEM500
|
4.1
|
40.2
|
1.0
|
C2D
|
A:HEM500
|
4.1
|
41.6
|
1.0
|
C3D
|
A:HEM500
|
4.1
|
38.9
|
1.0
|
CA
|
A:CYS394
|
4.1
|
37.6
|
1.0
|
C3A
|
A:HEM500
|
4.2
|
41.9
|
1.0
|
C2B
|
A:HEM500
|
4.2
|
45.0
|
1.0
|
C3C
|
A:HEM500
|
4.3
|
46.9
|
1.0
|
C3B
|
A:HEM500
|
4.3
|
47.0
|
1.0
|
O
|
A:GLY283
|
4.3
|
87.8
|
1.0
|
C2C
|
A:HEM500
|
4.3
|
48.9
|
1.0
|
CA
|
A:GLY283
|
4.8
|
74.7
|
1.0
|
C
|
A:GLY283
|
4.8
|
76.1
|
1.0
|
N
|
A:VAL395
|
4.9
|
43.9
|
1.0
|
N
|
A:GLY396
|
4.9
|
53.9
|
1.0
|
C
|
A:CYS394
|
4.9
|
40.5
|
1.0
|
|
Iron binding site 2 out
of 2 in 6hqw
Go back to
Iron Binding Sites List in 6hqw
Iron binding site 2 out
of 2 in the Cytochrome P450-153 From Novosphingobium Aromaticivorans
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Cytochrome P450-153 From Novosphingobium Aromaticivorans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe500
b:100.0
occ:1.00
|
FE
|
B:HEM500
|
0.0
|
100.0
|
1.0
|
ND
|
B:HEM500
|
1.9
|
98.3
|
1.0
|
NA
|
B:HEM500
|
2.0
|
89.8
|
1.0
|
SG
|
B:CYS394
|
2.1
|
80.6
|
1.0
|
NC
|
B:HEM500
|
2.1
|
89.0
|
1.0
|
NB
|
B:HEM500
|
2.1
|
97.6
|
1.0
|
C4D
|
B:HEM500
|
2.9
|
96.7
|
1.0
|
C1D
|
B:HEM500
|
2.9
|
91.9
|
1.0
|
C1A
|
B:HEM500
|
3.0
|
92.6
|
1.0
|
C4A
|
B:HEM500
|
3.0
|
91.3
|
1.0
|
C4C
|
B:HEM500
|
3.0
|
95.1
|
1.0
|
C1B
|
B:HEM500
|
3.1
|
93.9
|
1.0
|
C4B
|
B:HEM500
|
3.1
|
0.6
|
1.0
|
C1C
|
B:HEM500
|
3.1
|
90.0
|
1.0
|
CB
|
B:CYS394
|
3.3
|
81.2
|
1.0
|
CHA
|
B:HEM500
|
3.3
|
97.8
|
1.0
|
CHD
|
B:HEM500
|
3.4
|
98.4
|
1.0
|
CHB
|
B:HEM500
|
3.4
|
92.4
|
1.0
|
CHC
|
B:HEM500
|
3.5
|
94.0
|
1.0
|
O
|
B:GLY283
|
3.7
|
93.4
|
1.0
|
CA
|
B:CYS394
|
3.9
|
85.5
|
1.0
|
C3D
|
B:HEM500
|
4.1
|
90.1
|
1.0
|
C2D
|
B:HEM500
|
4.1
|
92.5
|
1.0
|
C3A
|
B:HEM500
|
4.2
|
91.7
|
1.0
|
C2A
|
B:HEM500
|
4.2
|
86.9
|
1.0
|
C3C
|
B:HEM500
|
4.3
|
94.8
|
1.0
|
C2C
|
B:HEM500
|
4.3
|
95.6
|
1.0
|
C2B
|
B:HEM500
|
4.3
|
95.1
|
1.0
|
C3B
|
B:HEM500
|
4.3
|
99.9
|
1.0
|
C
|
B:GLY283
|
4.4
|
93.4
|
1.0
|
CA
|
B:GLY283
|
4.5
|
92.8
|
1.0
|
C
|
B:CYS394
|
4.8
|
89.2
|
1.0
|
OG1
|
B:THR287
|
4.9
|
93.9
|
1.0
|
N
|
B:VAL395
|
4.9
|
97.0
|
1.0
|
|
Reference:
F.Fiorentini,
A.M.Hatzl,
S.Schmidt,
S.Savino,
A.Glieder,
A.Mattevi.
The Extreme Structural Plasticity in the CYP153 Subfamily of P450S Directs Development of Designer Hydroxylases. Biochemistry V. 57 6701 2018.
ISSN: ISSN 0006-2960
PubMed: 30398864
DOI: 10.1021/ACS.BIOCHEM.8B01052
Page generated: Sun Dec 13 16:29:01 2020
|