Iron in PDB 7con: Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine
Enzymatic activity of Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine
All present enzymatic activity of Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine:
1.14.14.1;
1.6.2.4;
Protein crystallography data
The structure of Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine, PDB code: 7con
was solved by
J.K.Stanfield,
H.Sugimoto,
O.Shoji,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
46.22 /
1.46
|
|
Space group
|
P 21 21 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
58.655,
128.189,
148.518,
90,
90,
90
|
|
R / Rfree (%)
|
15.4 /
18.8
|
Other elements in 7con:
The structure of Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine
(pdb code 7con). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine, PDB code: 7con:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 7con
Go back to
Iron Binding Sites List in 7con
Iron binding site 1 out
of 4 in the Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine
 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 CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:12.3
occ:0.50
|
FE
|
A:HEM501
|
0.0
|
12.3
|
0.5
|
|
FE
|
A:HEM501
|
0.0
|
12.4
|
0.5
|
|
ND
|
A:HEM501
|
1.9
|
12.4
|
0.5
|
|
ND
|
A:HEM501
|
2.0
|
12.4
|
0.5
|
|
NA
|
A:HEM501
|
2.0
|
12.5
|
0.5
|
|
NA
|
A:HEM501
|
2.0
|
12.1
|
0.5
|
|
ND
|
A:3CN502
|
2.1
|
14.3
|
0.4
|
|
NC
|
A:HEM501
|
2.1
|
12.1
|
0.5
|
|
NB
|
A:HEM501
|
2.1
|
11.8
|
0.5
|
|
NB
|
A:HEM501
|
2.1
|
12.7
|
0.5
|
|
NC
|
A:HEM501
|
2.1
|
11.8
|
0.5
|
|
ND
|
A:3CN502
|
2.2
|
19.5
|
0.6
|
|
SG
|
A:CYS400
|
2.3
|
13.0
|
1.0
|
|
C1D
|
A:HEM501
|
2.9
|
11.7
|
0.5
|
|
C4D
|
A:HEM501
|
3.0
|
11.4
|
0.5
|
|
C1D
|
A:HEM501
|
3.0
|
12.4
|
0.5
|
|
C4D
|
A:HEM501
|
3.0
|
12.0
|
0.5
|
|
C4C
|
A:HEM501
|
3.0
|
11.9
|
0.5
|
|
C1A
|
A:HEM501
|
3.0
|
11.4
|
0.5
|
|
C4A
|
A:HEM501
|
3.0
|
11.9
|
0.5
|
|
C1B
|
A:HEM501
|
3.0
|
12.7
|
0.5
|
|
C4B
|
A:HEM501
|
3.0
|
12.3
|
0.5
|
|
C4C
|
A:HEM501
|
3.1
|
12.3
|
0.5
|
|
C1B
|
A:HEM501
|
3.1
|
11.7
|
0.5
|
|
C1A
|
A:HEM501
|
3.1
|
11.6
|
0.5
|
|
C4B
|
A:HEM501
|
3.1
|
13.1
|
0.5
|
|
C4A
|
A:HEM501
|
3.1
|
12.1
|
0.5
|
|
C1C
|
A:HEM501
|
3.1
|
12.1
|
0.5
|
|
C1C
|
A:HEM501
|
3.1
|
12.7
|
0.5
|
|
CC
|
A:3CN502
|
3.3
|
14.1
|
0.4
|
|
CC
|
A:3CN502
|
3.4
|
20.8
|
0.6
|
|
CHD
|
A:HEM501
|
3.4
|
11.9
|
0.5
|
|
CB
|
A:CYS400
|
3.4
|
11.2
|
1.0
|
|
CHB
|
A:HEM501
|
3.4
|
12.5
|
0.5
|
|
CHA
|
A:HEM501
|
3.4
|
12.2
|
0.5
|
|
CHA
|
A:HEM501
|
3.4
|
11.9
|
0.5
|
|
CHD
|
A:HEM501
|
3.4
|
12.9
|
0.5
|
|
CHC
|
A:HEM501
|
3.5
|
12.5
|
0.5
|
|
CHC
|
A:HEM501
|
3.5
|
13.0
|
0.5
|
|
CHB
|
A:HEM501
|
3.5
|
12.0
|
0.5
|
|
CA
|
A:CYS400
|
4.1
|
11.3
|
1.0
|
|
C2D
|
A:HEM501
|
4.2
|
12.2
|
0.5
|
|
C3A
|
A:HEM501
|
4.2
|
12.5
|
0.5
|
|
C3D
|
A:HEM501
|
4.2
|
12.2
|
0.5
|
|
C2A
|
A:HEM501
|
4.2
|
11.9
|
0.5
|
|
C3C
|
A:HEM501
|
4.2
|
11.9
|
0.5
|
|
C2D
|
A:HEM501
|
4.3
|
12.0
|
0.5
|
|
C3C
|
A:HEM501
|
4.3
|
13.0
|
0.5
|
|
C2B
|
A:HEM501
|
4.3
|
13.5
|
0.5
|
|
C3D
|
A:HEM501
|
4.3
|
12.1
|
0.5
|
|
C2B
|
A:HEM501
|
4.3
|
11.9
|
0.5
|
|
C2C
|
A:HEM501
|
4.3
|
11.4
|
0.5
|
|
C2C
|
A:HEM501
|
4.3
|
12.7
|
0.5
|
|
C2A
|
A:HEM501
|
4.3
|
11.6
|
0.5
|
|
C3A
|
A:HEM501
|
4.3
|
11.6
|
0.5
|
|
C3B
|
A:HEM501
|
4.3
|
12.1
|
0.5
|
|
C3B
|
A:HEM501
|
4.3
|
13.2
|
0.5
|
|
CB
|
A:3CN502
|
4.5
|
16.1
|
0.4
|
|
CB
|
A:3CN502
|
4.6
|
23.6
|
0.6
|
|
CA
|
A:3CN502
|
4.8
|
16.0
|
0.4
|
|
N
|
A:GLY402
|
4.8
|
12.2
|
1.0
|
|
C
|
A:CYS400
|
4.8
|
11.1
|
1.0
|
|
N
|
A:ILE401
|
5.0
|
11.2
|
1.0
|
|
Iron binding site 2 out
of 4 in 7con
Go back to
Iron Binding Sites List in 7con
Iron binding site 2 out
of 4 in the Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine
 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 CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:12.4
occ:0.50
|
FE
|
A:HEM501
|
0.0
|
12.4
|
0.5
|
|
FE
|
A:HEM501
|
0.0
|
12.3
|
0.5
|
|
ND
|
A:HEM501
|
1.9
|
12.4
|
0.5
|
|
ND
|
A:HEM501
|
2.0
|
12.4
|
0.5
|
|
NA
|
A:HEM501
|
2.0
|
12.1
|
0.5
|
|
NA
|
A:HEM501
|
2.0
|
12.5
|
0.5
|
|
NB
|
A:HEM501
|
2.0
|
11.8
|
0.5
|
|
NC
|
A:HEM501
|
2.1
|
11.8
|
0.5
|
|
NC
|
A:HEM501
|
2.1
|
12.1
|
0.5
|
|
ND
|
A:3CN502
|
2.1
|
14.3
|
0.4
|
|
NB
|
A:HEM501
|
2.1
|
12.7
|
0.5
|
|
ND
|
A:3CN502
|
2.2
|
19.5
|
0.6
|
|
SG
|
A:CYS400
|
2.3
|
13.0
|
1.0
|
|
C1D
|
A:HEM501
|
2.9
|
12.4
|
0.5
|
|
C1D
|
A:HEM501
|
3.0
|
11.7
|
0.5
|
|
C4D
|
A:HEM501
|
3.0
|
12.0
|
0.5
|
|
C4D
|
A:HEM501
|
3.0
|
11.4
|
0.5
|
|
C4B
|
A:HEM501
|
3.0
|
12.3
|
0.5
|
|
C4C
|
A:HEM501
|
3.0
|
12.3
|
0.5
|
|
C1B
|
A:HEM501
|
3.0
|
11.7
|
0.5
|
|
C1A
|
A:HEM501
|
3.0
|
11.4
|
0.5
|
|
C4C
|
A:HEM501
|
3.0
|
11.9
|
0.5
|
|
C1A
|
A:HEM501
|
3.1
|
11.6
|
0.5
|
|
C1B
|
A:HEM501
|
3.1
|
12.7
|
0.5
|
|
C4A
|
A:HEM501
|
3.1
|
11.9
|
0.5
|
|
C4A
|
A:HEM501
|
3.1
|
12.1
|
0.5
|
|
C4B
|
A:HEM501
|
3.1
|
13.1
|
0.5
|
|
C1C
|
A:HEM501
|
3.1
|
12.7
|
0.5
|
|
C1C
|
A:HEM501
|
3.1
|
12.1
|
0.5
|
|
CC
|
A:3CN502
|
3.3
|
14.1
|
0.4
|
|
CB
|
A:CYS400
|
3.3
|
11.2
|
1.0
|
|
CC
|
A:3CN502
|
3.4
|
20.8
|
0.6
|
|
CHD
|
A:HEM501
|
3.4
|
12.9
|
0.5
|
|
CHD
|
A:HEM501
|
3.4
|
11.9
|
0.5
|
|
CHA
|
A:HEM501
|
3.4
|
12.2
|
0.5
|
|
CHA
|
A:HEM501
|
3.4
|
11.9
|
0.5
|
|
CHC
|
A:HEM501
|
3.4
|
12.5
|
0.5
|
|
CHB
|
A:HEM501
|
3.4
|
12.5
|
0.5
|
|
CHB
|
A:HEM501
|
3.5
|
12.0
|
0.5
|
|
CHC
|
A:HEM501
|
3.5
|
13.0
|
0.5
|
|
CA
|
A:CYS400
|
4.0
|
11.3
|
1.0
|
|
C3C
|
A:HEM501
|
4.2
|
13.0
|
0.5
|
|
C2D
|
A:HEM501
|
4.2
|
12.0
|
0.5
|
|
C2B
|
A:HEM501
|
4.2
|
11.9
|
0.5
|
|
C2D
|
A:HEM501
|
4.2
|
12.2
|
0.5
|
|
C3D
|
A:HEM501
|
4.3
|
12.2
|
0.5
|
|
C2A
|
A:HEM501
|
4.3
|
11.9
|
0.5
|
|
C3D
|
A:HEM501
|
4.3
|
12.1
|
0.5
|
|
C3A
|
A:HEM501
|
4.3
|
12.5
|
0.5
|
|
C2C
|
A:HEM501
|
4.3
|
12.7
|
0.5
|
|
C3B
|
A:HEM501
|
4.3
|
12.1
|
0.5
|
|
C3A
|
A:HEM501
|
4.3
|
11.6
|
0.5
|
|
C3C
|
A:HEM501
|
4.3
|
11.9
|
0.5
|
|
C2A
|
A:HEM501
|
4.3
|
11.6
|
0.5
|
|
C2C
|
A:HEM501
|
4.3
|
11.4
|
0.5
|
|
C2B
|
A:HEM501
|
4.3
|
13.5
|
0.5
|
|
C3B
|
A:HEM501
|
4.3
|
13.2
|
0.5
|
|
CB
|
A:3CN502
|
4.6
|
16.1
|
0.4
|
|
CB
|
A:3CN502
|
4.7
|
23.6
|
0.6
|
|
CA
|
A:3CN502
|
4.8
|
16.0
|
0.4
|
|
N
|
A:GLY402
|
4.8
|
12.2
|
1.0
|
|
C
|
A:CYS400
|
4.8
|
11.1
|
1.0
|
|
N
|
A:ILE401
|
5.0
|
11.2
|
1.0
|
|
Iron binding site 3 out
of 4 in 7con
Go back to
Iron Binding Sites List in 7con
Iron binding site 3 out
of 4 in the Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine
 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 CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe501
b:13.3
occ:0.50
|
FE
|
B:HEM501
|
0.0
|
13.3
|
0.5
|
|
FE
|
B:HEM501
|
0.0
|
13.2
|
0.5
|
|
ND
|
B:HEM501
|
1.9
|
12.8
|
0.5
|
|
ND
|
B:HEM501
|
2.0
|
12.8
|
0.5
|
|
ND
|
B:3CN502
|
2.0
|
10.0
|
0.2
|
|
NA
|
B:HEM501
|
2.0
|
12.6
|
0.5
|
|
NA
|
B:HEM501
|
2.0
|
12.4
|
0.5
|
|
NC
|
B:HEM501
|
2.1
|
12.9
|
0.5
|
|
NB
|
B:HEM501
|
2.1
|
13.3
|
0.5
|
|
NB
|
B:HEM501
|
2.1
|
12.7
|
0.5
|
|
NC
|
B:HEM501
|
2.1
|
12.6
|
0.5
|
|
ND
|
B:3CN502
|
2.2
|
17.3
|
0.8
|
|
SG
|
B:CYS400
|
2.3
|
14.2
|
1.0
|
|
C1D
|
B:HEM501
|
2.9
|
12.8
|
0.5
|
|
C4D
|
B:HEM501
|
2.9
|
12.4
|
0.5
|
|
C1D
|
B:HEM501
|
3.0
|
12.7
|
0.5
|
|
C4D
|
B:HEM501
|
3.0
|
12.6
|
0.5
|
|
C1A
|
B:HEM501
|
3.0
|
12.4
|
0.5
|
|
C4B
|
B:HEM501
|
3.0
|
13.1
|
0.5
|
|
C4C
|
B:HEM501
|
3.0
|
13.5
|
0.5
|
|
C4C
|
B:HEM501
|
3.0
|
13.4
|
0.5
|
|
C4A
|
B:HEM501
|
3.0
|
12.9
|
0.5
|
|
C4B
|
B:HEM501
|
3.0
|
12.9
|
0.5
|
|
C1B
|
B:HEM501
|
3.1
|
13.3
|
0.5
|
|
C1B
|
B:HEM501
|
3.1
|
13.0
|
0.5
|
|
C1A
|
B:HEM501
|
3.1
|
12.3
|
0.5
|
|
C4A
|
B:HEM501
|
3.1
|
12.5
|
0.5
|
|
C1C
|
B:HEM501
|
3.1
|
13.0
|
0.5
|
|
C1C
|
B:HEM501
|
3.1
|
12.6
|
0.5
|
|
CC
|
B:3CN502
|
3.2
|
10.6
|
0.2
|
|
CC
|
B:3CN502
|
3.4
|
20.6
|
0.8
|
|
CHD
|
B:HEM501
|
3.4
|
13.6
|
0.5
|
|
CB
|
B:CYS400
|
3.4
|
13.3
|
1.0
|
|
CHD
|
B:HEM501
|
3.4
|
13.7
|
0.5
|
|
CHA
|
B:HEM501
|
3.4
|
12.8
|
0.5
|
|
CHA
|
B:HEM501
|
3.4
|
12.6
|
0.5
|
|
CHB
|
B:HEM501
|
3.4
|
13.3
|
0.5
|
|
CHC
|
B:HEM501
|
3.4
|
13.9
|
0.5
|
|
CHC
|
B:HEM501
|
3.5
|
13.5
|
0.5
|
|
CHB
|
B:HEM501
|
3.5
|
13.6
|
0.5
|
|
CA
|
B:CYS400
|
4.0
|
12.3
|
1.0
|
|
C2D
|
B:HEM501
|
4.2
|
13.1
|
0.5
|
|
C3D
|
B:HEM501
|
4.2
|
12.9
|
0.5
|
|
C3A
|
B:HEM501
|
4.2
|
13.4
|
0.5
|
|
C2A
|
B:HEM501
|
4.2
|
12.9
|
0.5
|
|
C3C
|
B:HEM501
|
4.2
|
13.5
|
0.5
|
|
C2D
|
B:HEM501
|
4.3
|
12.8
|
0.5
|
|
C3C
|
B:HEM501
|
4.3
|
13.5
|
0.5
|
|
C2C
|
B:HEM501
|
4.3
|
12.5
|
0.5
|
|
C2C
|
B:HEM501
|
4.3
|
13.4
|
0.5
|
|
C3B
|
B:HEM501
|
4.3
|
13.2
|
0.5
|
|
C2B
|
B:HEM501
|
4.3
|
13.2
|
0.5
|
|
C2B
|
B:HEM501
|
4.3
|
12.5
|
0.5
|
|
C3D
|
B:HEM501
|
4.3
|
13.0
|
0.5
|
|
C3A
|
B:HEM501
|
4.3
|
12.6
|
0.5
|
|
C2A
|
B:HEM501
|
4.3
|
12.6
|
0.5
|
|
C3B
|
B:HEM501
|
4.3
|
13.0
|
0.5
|
|
CB
|
B:3CN502
|
4.4
|
11.4
|
0.2
|
|
CB
|
B:3CN502
|
4.7
|
26.5
|
0.8
|
|
N
|
B:GLY402
|
4.8
|
14.2
|
1.0
|
|
CA
|
B:3CN502
|
4.8
|
11.0
|
0.2
|
|
C
|
B:CYS400
|
4.8
|
12.9
|
1.0
|
|
N
|
B:ILE401
|
5.0
|
13.6
|
1.0
|
|
Iron binding site 4 out
of 4 in 7con
Go back to
Iron Binding Sites List in 7con
Iron binding site 4 out
of 4 in the Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine
 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 CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy) Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe501
b:13.2
occ:0.50
|
FE
|
B:HEM501
|
0.0
|
13.2
|
0.5
|
|
FE
|
B:HEM501
|
0.0
|
13.3
|
0.5
|
|
ND
|
B:HEM501
|
1.9
|
12.8
|
0.5
|
|
ND
|
B:HEM501
|
1.9
|
12.8
|
0.5
|
|
ND
|
B:3CN502
|
2.0
|
10.0
|
0.2
|
|
NA
|
B:HEM501
|
2.0
|
12.4
|
0.5
|
|
NA
|
B:HEM501
|
2.0
|
12.6
|
0.5
|
|
NB
|
B:HEM501
|
2.0
|
13.3
|
0.5
|
|
NC
|
B:HEM501
|
2.0
|
12.6
|
0.5
|
|
NC
|
B:HEM501
|
2.1
|
12.9
|
0.5
|
|
NB
|
B:HEM501
|
2.1
|
12.7
|
0.5
|
|
ND
|
B:3CN502
|
2.2
|
17.3
|
0.8
|
|
SG
|
B:CYS400
|
2.3
|
14.2
|
1.0
|
|
C1D
|
B:HEM501
|
2.9
|
12.7
|
0.5
|
|
C1D
|
B:HEM501
|
2.9
|
12.8
|
0.5
|
|
C4D
|
B:HEM501
|
3.0
|
12.4
|
0.5
|
|
C4D
|
B:HEM501
|
3.0
|
12.6
|
0.5
|
|
C4C
|
B:HEM501
|
3.0
|
13.5
|
0.5
|
|
C4B
|
B:HEM501
|
3.0
|
13.1
|
0.5
|
|
C1B
|
B:HEM501
|
3.0
|
13.3
|
0.5
|
|
C1A
|
B:HEM501
|
3.0
|
12.4
|
0.5
|
|
C4B
|
B:HEM501
|
3.1
|
12.9
|
0.5
|
|
C1A
|
B:HEM501
|
3.1
|
12.3
|
0.5
|
|
C4A
|
B:HEM501
|
3.1
|
12.5
|
0.5
|
|
C4C
|
B:HEM501
|
3.1
|
13.4
|
0.5
|
|
C4A
|
B:HEM501
|
3.1
|
12.9
|
0.5
|
|
C1C
|
B:HEM501
|
3.1
|
12.6
|
0.5
|
|
C1B
|
B:HEM501
|
3.1
|
13.0
|
0.5
|
|
C1C
|
B:HEM501
|
3.1
|
13.0
|
0.5
|
|
CC
|
B:3CN502
|
3.2
|
10.6
|
0.2
|
|
CB
|
B:CYS400
|
3.3
|
13.3
|
1.0
|
|
CHD
|
B:HEM501
|
3.4
|
13.7
|
0.5
|
|
CC
|
B:3CN502
|
3.4
|
20.6
|
0.8
|
|
CHD
|
B:HEM501
|
3.4
|
13.6
|
0.5
|
|
CHA
|
B:HEM501
|
3.4
|
12.8
|
0.5
|
|
CHA
|
B:HEM501
|
3.4
|
12.6
|
0.5
|
|
CHB
|
B:HEM501
|
3.4
|
13.6
|
0.5
|
|
CHC
|
B:HEM501
|
3.4
|
13.9
|
0.5
|
|
CHC
|
B:HEM501
|
3.5
|
13.5
|
0.5
|
|
CHB
|
B:HEM501
|
3.5
|
13.3
|
0.5
|
|
CA
|
B:CYS400
|
4.0
|
12.3
|
1.0
|
|
C2D
|
B:HEM501
|
4.2
|
13.1
|
0.5
|
|
C3C
|
B:HEM501
|
4.2
|
13.5
|
0.5
|
|
C3D
|
B:HEM501
|
4.2
|
12.9
|
0.5
|
|
C2D
|
B:HEM501
|
4.2
|
12.8
|
0.5
|
|
C2A
|
B:HEM501
|
4.2
|
12.9
|
0.5
|
|
C2C
|
B:HEM501
|
4.2
|
12.5
|
0.5
|
|
C3A
|
B:HEM501
|
4.2
|
13.4
|
0.5
|
|
C2B
|
B:HEM501
|
4.2
|
13.2
|
0.5
|
|
C3B
|
B:HEM501
|
4.3
|
13.2
|
0.5
|
|
C3A
|
B:HEM501
|
4.3
|
12.6
|
0.5
|
|
C3D
|
B:HEM501
|
4.3
|
13.0
|
0.5
|
|
C2A
|
B:HEM501
|
4.3
|
12.6
|
0.5
|
|
C3C
|
B:HEM501
|
4.3
|
13.5
|
0.5
|
|
C2C
|
B:HEM501
|
4.3
|
13.4
|
0.5
|
|
C2B
|
B:HEM501
|
4.3
|
12.5
|
0.5
|
|
C3B
|
B:HEM501
|
4.3
|
13.0
|
0.5
|
|
CB
|
B:3CN502
|
4.5
|
11.4
|
0.2
|
|
CB
|
B:3CN502
|
4.7
|
26.5
|
0.8
|
|
N
|
B:GLY402
|
4.8
|
14.2
|
1.0
|
|
CA
|
B:3CN502
|
4.8
|
11.0
|
0.2
|
|
C
|
B:CYS400
|
4.8
|
12.9
|
1.0
|
|
N
|
B:ILE401
|
5.0
|
13.6
|
1.0
|
|
Reference:
O.Shoji,
J.K.Stanfield.
Structure of the CYP102A1 Haem Domain with N-{2-[4-(Trifluoromethoxy)Phenoxy]}Acetoyl-L-Phenylalanine in Complex with N-Propylamine at 1.46 Angstrom Resolution To Be Published.
Page generated: Fri Sep 24 14:02:47 2021
|
