Fluorine in PDB 8oie: Iron Nitrogenase Complex From Rhodobacter Capsulatus
Enzymatic activity of Iron Nitrogenase Complex From Rhodobacter Capsulatus
All present enzymatic activity of Iron Nitrogenase Complex From Rhodobacter Capsulatus:
1.18.6.1;
Other elements in 8oie:
The structure of Iron Nitrogenase Complex From Rhodobacter Capsulatus also contains other interesting chemical elements:
Fluorine Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Fluorine atom in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
(pdb code 8oie). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 12 binding sites of Fluorine where determined in the
Iron Nitrogenase Complex From Rhodobacter Capsulatus, PDB code: 8oie:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Fluorine binding site 1 out
of 12 in 8oie
Go back to
Fluorine Binding Sites List in 8oie
Fluorine binding site 1 out
of 12 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:F303
b:79.3
occ:1.00
|
F1
|
D:AF3303
|
0.0
|
79.3
|
1.0
|
AL
|
D:AF3303
|
1.8
|
62.1
|
1.0
|
MG
|
D:MG302
|
2.3
|
60.1
|
1.0
|
O1B
|
D:ADP301
|
2.4
|
69.0
|
1.0
|
O2B
|
D:ADP301
|
2.9
|
68.2
|
1.0
|
PB
|
D:ADP301
|
3.0
|
55.6
|
1.0
|
F2
|
D:AF3303
|
3.1
|
73.4
|
1.0
|
F3
|
D:AF3303
|
3.1
|
73.7
|
1.0
|
OD2
|
D:ASP40
|
3.4
|
72.8
|
1.0
|
O3B
|
D:ADP301
|
3.7
|
48.9
|
1.0
|
CE
|
D:LYS15
|
3.7
|
44.6
|
1.0
|
CA
|
D:LEU127
|
3.9
|
46.6
|
1.0
|
O
|
D:VAL126
|
3.9
|
65.5
|
1.0
|
NZ
|
D:LYS15
|
4.0
|
49.6
|
1.0
|
N
|
D:GLY128
|
4.3
|
55.4
|
1.0
|
C
|
D:LEU127
|
4.3
|
55.9
|
1.0
|
NZ
|
D:LYS42
|
4.3
|
62.6
|
1.0
|
OG
|
D:SER16
|
4.4
|
60.3
|
1.0
|
CG
|
D:ASP40
|
4.5
|
70.1
|
1.0
|
O3A
|
D:ADP301
|
4.5
|
61.5
|
1.0
|
C
|
D:VAL126
|
4.7
|
56.0
|
1.0
|
N
|
D:LEU127
|
4.7
|
58.9
|
1.0
|
CB
|
D:LEU127
|
4.8
|
45.3
|
1.0
|
CB
|
D:LYS15
|
4.9
|
47.0
|
1.0
|
|
Fluorine binding site 2 out
of 12 in 8oie
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Fluorine Binding Sites List in 8oie
Fluorine binding site 2 out
of 12 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:F303
b:73.4
occ:1.00
|
F2
|
D:AF3303
|
0.0
|
73.4
|
1.0
|
AL
|
D:AF3303
|
1.8
|
62.1
|
1.0
|
O1B
|
D:ADP301
|
2.8
|
69.0
|
1.0
|
N
|
D:GLY12
|
3.0
|
48.2
|
1.0
|
CA
|
D:GLY11
|
3.0
|
50.3
|
1.0
|
NZ
|
D:LYS15
|
3.0
|
49.6
|
1.0
|
F3
|
D:AF3303
|
3.1
|
73.7
|
1.0
|
F1
|
D:AF3303
|
3.1
|
79.3
|
1.0
|
N
|
D:GLY128
|
3.3
|
55.4
|
1.0
|
CA
|
D:GLY128
|
3.4
|
49.0
|
1.0
|
C
|
D:GLY11
|
3.5
|
49.3
|
1.0
|
O3B
|
D:ADP301
|
3.8
|
48.9
|
1.0
|
CE
|
D:LYS15
|
3.8
|
44.6
|
1.0
|
PB
|
D:ADP301
|
3.8
|
55.6
|
1.0
|
OD2
|
E:ASP129
|
3.9
|
74.4
|
1.0
|
O
|
D:LYS10
|
4.0
|
52.6
|
1.0
|
N
|
D:GLY11
|
4.1
|
54.3
|
1.0
|
CA
|
D:GLY12
|
4.1
|
51.4
|
1.0
|
C
|
D:LEU127
|
4.2
|
55.9
|
1.0
|
C
|
D:LYS10
|
4.5
|
49.2
|
1.0
|
C
|
D:GLY128
|
4.6
|
55.8
|
1.0
|
CA
|
D:LEU127
|
4.7
|
46.6
|
1.0
|
O
|
D:GLY11
|
4.7
|
60.8
|
1.0
|
O2B
|
D:ADP301
|
4.8
|
68.2
|
1.0
|
CG
|
E:ASP129
|
4.8
|
73.3
|
1.0
|
OD1
|
E:ASP129
|
4.8
|
70.3
|
1.0
|
CA
|
E:GLY11
|
4.9
|
54.6
|
1.0
|
|
Fluorine binding site 3 out
of 12 in 8oie
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Fluorine Binding Sites List in 8oie
Fluorine binding site 3 out
of 12 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:F303
b:73.7
occ:1.00
|
F3
|
D:AF3303
|
0.0
|
73.7
|
1.0
|
AL
|
D:AF3303
|
1.8
|
62.1
|
1.0
|
O1B
|
D:ADP301
|
2.6
|
69.0
|
1.0
|
NZ
|
D:LYS42
|
2.7
|
62.6
|
1.0
|
F2
|
D:AF3303
|
3.1
|
73.4
|
1.0
|
NZ
|
E:LYS10
|
3.1
|
56.4
|
1.0
|
F1
|
D:AF3303
|
3.1
|
79.3
|
1.0
|
CE
|
D:LYS42
|
3.8
|
63.3
|
1.0
|
CE
|
E:LYS10
|
3.8
|
57.5
|
1.0
|
PB
|
D:ADP301
|
4.1
|
55.6
|
1.0
|
OD1
|
E:ASP129
|
4.1
|
70.3
|
1.0
|
OD2
|
D:ASP40
|
4.1
|
72.8
|
1.0
|
CG
|
E:LYS10
|
4.3
|
61.8
|
1.0
|
N
|
D:GLY12
|
4.5
|
48.2
|
1.0
|
MG
|
D:MG302
|
4.5
|
60.1
|
1.0
|
O2B
|
D:ADP301
|
4.7
|
68.2
|
1.0
|
OD2
|
E:ASP129
|
4.7
|
74.4
|
1.0
|
CD
|
E:LYS10
|
4.7
|
58.4
|
1.0
|
N
|
E:GLY11
|
4.8
|
57.0
|
1.0
|
O3A
|
D:ADP301
|
4.8
|
61.5
|
1.0
|
CG
|
E:ASP129
|
4.8
|
73.3
|
1.0
|
CA
|
D:GLY12
|
4.8
|
51.4
|
1.0
|
CD
|
D:LYS42
|
4.9
|
64.6
|
1.0
|
OD2
|
D:ASP44
|
5.0
|
73.9
|
1.0
|
|
Fluorine binding site 4 out
of 12 in 8oie
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Fluorine Binding Sites List in 8oie
Fluorine binding site 4 out
of 12 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:F303
b:74.6
occ:1.00
|
F1
|
E:AF3303
|
0.0
|
74.6
|
1.0
|
AL
|
E:AF3303
|
1.8
|
60.3
|
1.0
|
MG
|
E:MG302
|
2.3
|
58.4
|
1.0
|
O3B
|
E:ADP301
|
2.7
|
60.6
|
1.0
|
OD2
|
E:ASP40
|
3.1
|
75.3
|
1.0
|
F3
|
E:AF3303
|
3.1
|
72.3
|
1.0
|
F2
|
E:AF3303
|
3.1
|
82.1
|
1.0
|
O2B
|
E:ADP301
|
3.2
|
69.6
|
1.0
|
PB
|
E:ADP301
|
3.4
|
62.5
|
1.0
|
CA
|
E:LEU127
|
3.8
|
54.5
|
1.0
|
NZ
|
E:LYS42
|
4.0
|
67.9
|
1.0
|
CG
|
E:ASP40
|
4.1
|
69.9
|
1.0
|
O1B
|
E:ADP301
|
4.2
|
61.4
|
1.0
|
CE
|
E:LYS15
|
4.2
|
51.2
|
1.0
|
CB
|
E:LEU127
|
4.4
|
52.0
|
1.0
|
OG
|
E:SER16
|
4.4
|
66.1
|
1.0
|
N
|
E:GLY128
|
4.4
|
50.6
|
1.0
|
O
|
E:VAL126
|
4.4
|
68.3
|
1.0
|
C
|
E:LEU127
|
4.5
|
55.3
|
1.0
|
NZ
|
E:LYS15
|
4.5
|
45.0
|
1.0
|
N
|
E:LEU127
|
4.6
|
56.3
|
1.0
|
CB
|
E:ASP40
|
4.8
|
61.9
|
1.0
|
O3A
|
E:ADP301
|
4.8
|
61.8
|
1.0
|
C
|
E:VAL126
|
4.9
|
55.8
|
1.0
|
OD1
|
E:ASP44
|
5.0
|
83.1
|
1.0
|
OD1
|
D:ASP129
|
5.0
|
61.2
|
1.0
|
OD1
|
E:ASP40
|
5.0
|
70.0
|
1.0
|
NZ
|
D:LYS10
|
5.0
|
43.4
|
1.0
|
|
Fluorine binding site 5 out
of 12 in 8oie
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Fluorine Binding Sites List in 8oie
Fluorine binding site 5 out
of 12 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 5 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:F303
b:82.1
occ:1.00
|
F2
|
E:AF3303
|
0.0
|
82.1
|
1.0
|
AL
|
E:AF3303
|
1.8
|
60.3
|
1.0
|
O3B
|
E:ADP301
|
2.7
|
60.6
|
1.0
|
NZ
|
E:LYS15
|
2.8
|
45.0
|
1.0
|
CA
|
E:GLY11
|
2.9
|
54.6
|
1.0
|
N
|
E:GLY12
|
2.9
|
56.5
|
1.0
|
F1
|
E:AF3303
|
3.1
|
74.6
|
1.0
|
F3
|
E:AF3303
|
3.1
|
72.3
|
1.0
|
N
|
E:GLY128
|
3.3
|
50.6
|
1.0
|
C
|
E:GLY11
|
3.4
|
58.5
|
1.0
|
CA
|
E:GLY128
|
3.6
|
52.5
|
1.0
|
CE
|
E:LYS15
|
3.6
|
51.2
|
1.0
|
O1B
|
E:ADP301
|
3.6
|
61.4
|
1.0
|
PB
|
E:ADP301
|
3.6
|
62.5
|
1.0
|
N
|
E:GLY11
|
4.0
|
57.0
|
1.0
|
O
|
E:LYS10
|
4.1
|
72.7
|
1.0
|
CA
|
E:GLY12
|
4.1
|
47.5
|
1.0
|
C
|
E:LEU127
|
4.1
|
55.3
|
1.0
|
OD2
|
D:ASP129
|
4.4
|
70.0
|
1.0
|
C
|
E:LYS10
|
4.4
|
66.8
|
1.0
|
CA
|
E:LEU127
|
4.5
|
54.5
|
1.0
|
O2B
|
E:ADP301
|
4.5
|
69.6
|
1.0
|
O
|
E:GLY11
|
4.6
|
68.2
|
1.0
|
C
|
E:GLY128
|
4.9
|
56.4
|
1.0
|
O3A
|
E:ADP301
|
4.9
|
61.8
|
1.0
|
OD1
|
D:ASP129
|
4.9
|
61.2
|
1.0
|
CA
|
D:GLY11
|
4.9
|
50.3
|
1.0
|
MG
|
E:MG302
|
4.9
|
58.4
|
1.0
|
|
Fluorine binding site 6 out
of 12 in 8oie
Go back to
Fluorine Binding Sites List in 8oie
Fluorine binding site 6 out
of 12 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 6 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:F303
b:72.3
occ:1.00
|
F3
|
E:AF3303
|
0.0
|
72.3
|
1.0
|
AL
|
E:AF3303
|
1.8
|
60.3
|
1.0
|
O3B
|
E:ADP301
|
2.3
|
60.6
|
1.0
|
NZ
|
D:LYS10
|
2.7
|
43.4
|
1.0
|
F1
|
E:AF3303
|
3.1
|
74.6
|
1.0
|
F2
|
E:AF3303
|
3.1
|
82.1
|
1.0
|
NZ
|
E:LYS42
|
3.2
|
67.9
|
1.0
|
CE
|
D:LYS10
|
3.3
|
41.9
|
1.0
|
PB
|
E:ADP301
|
3.7
|
62.5
|
1.0
|
CG
|
D:LYS10
|
3.9
|
48.6
|
1.0
|
N
|
E:GLY12
|
4.0
|
56.5
|
1.0
|
CD
|
D:LYS10
|
4.2
|
45.9
|
1.0
|
CE
|
E:LYS42
|
4.4
|
64.1
|
1.0
|
CA
|
E:GLY12
|
4.4
|
47.5
|
1.0
|
O3A
|
E:ADP301
|
4.4
|
61.8
|
1.0
|
N
|
D:GLY11
|
4.4
|
54.3
|
1.0
|
O2B
|
E:ADP301
|
4.4
|
69.6
|
1.0
|
MG
|
E:MG302
|
4.6
|
58.4
|
1.0
|
OD2
|
E:ASP40
|
4.6
|
75.3
|
1.0
|
OD1
|
D:ASP129
|
4.7
|
61.2
|
1.0
|
O1B
|
E:ADP301
|
4.7
|
61.4
|
1.0
|
CA
|
D:GLY11
|
4.8
|
50.3
|
1.0
|
O2A
|
E:ADP301
|
4.9
|
66.2
|
1.0
|
C
|
E:GLY11
|
5.0
|
58.5
|
1.0
|
|
Fluorine binding site 7 out
of 12 in 8oie
Go back to
Fluorine Binding Sites List in 8oie
Fluorine binding site 7 out
of 12 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 7 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:F303
b:76.6
occ:1.00
|
F1
|
I:AF3303
|
0.0
|
76.6
|
1.0
|
AL
|
I:AF3303
|
1.8
|
61.5
|
1.0
|
O1B
|
I:ADP301
|
2.4
|
68.6
|
1.0
|
MG
|
I:MG302
|
2.5
|
56.1
|
1.0
|
F3
|
I:AF3303
|
3.1
|
71.1
|
1.0
|
F2
|
I:AF3303
|
3.1
|
70.9
|
1.0
|
O2B
|
I:ADP301
|
3.1
|
67.7
|
1.0
|
PB
|
I:ADP301
|
3.2
|
54.2
|
1.0
|
OD2
|
I:ASP40
|
3.2
|
72.5
|
1.0
|
CA
|
I:LEU127
|
3.7
|
46.7
|
1.0
|
CE
|
I:LYS15
|
3.8
|
44.7
|
1.0
|
O3B
|
I:ADP301
|
3.9
|
48.2
|
1.0
|
O
|
I:VAL126
|
4.0
|
66.7
|
1.0
|
N
|
I:GLY128
|
4.1
|
54.5
|
1.0
|
NZ
|
I:LYS15
|
4.1
|
49.5
|
1.0
|
C
|
I:LEU127
|
4.2
|
55.6
|
1.0
|
NZ
|
I:LYS42
|
4.2
|
62.9
|
1.0
|
CG
|
I:ASP40
|
4.3
|
70.1
|
1.0
|
OG
|
I:SER16
|
4.5
|
59.5
|
1.0
|
N
|
I:LEU127
|
4.6
|
56.8
|
1.0
|
CB
|
I:LEU127
|
4.6
|
45.9
|
1.0
|
O3A
|
I:ADP301
|
4.6
|
61.0
|
1.0
|
C
|
I:VAL126
|
4.7
|
55.5
|
1.0
|
CB
|
I:ASP40
|
5.0
|
63.6
|
1.0
|
|
Fluorine binding site 8 out
of 12 in 8oie
Go back to
Fluorine Binding Sites List in 8oie
Fluorine binding site 8 out
of 12 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 8 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:F303
b:70.9
occ:1.00
|
F2
|
I:AF3303
|
0.0
|
70.9
|
1.0
|
AL
|
I:AF3303
|
1.8
|
61.5
|
1.0
|
O1B
|
I:ADP301
|
2.6
|
68.6
|
1.0
|
N
|
I:GLY12
|
2.8
|
49.3
|
1.0
|
CA
|
I:GLY11
|
2.9
|
50.5
|
1.0
|
NZ
|
I:LYS15
|
3.0
|
49.5
|
1.0
|
F3
|
I:AF3303
|
3.1
|
71.1
|
1.0
|
F1
|
I:AF3303
|
3.1
|
76.6
|
1.0
|
N
|
I:GLY128
|
3.4
|
54.5
|
1.0
|
C
|
I:GLY11
|
3.4
|
50.0
|
1.0
|
CA
|
I:GLY128
|
3.5
|
49.2
|
1.0
|
O3B
|
I:ADP301
|
3.7
|
48.2
|
1.0
|
PB
|
I:ADP301
|
3.7
|
54.2
|
1.0
|
CE
|
I:LYS15
|
3.8
|
44.7
|
1.0
|
O
|
I:LYS10
|
4.0
|
52.9
|
1.0
|
CA
|
I:GLY12
|
4.0
|
50.7
|
1.0
|
OD2
|
J:ASP129
|
4.0
|
77.7
|
1.0
|
N
|
I:GLY11
|
4.1
|
54.0
|
1.0
|
C
|
I:LEU127
|
4.3
|
55.6
|
1.0
|
C
|
I:LYS10
|
4.4
|
49.8
|
1.0
|
O
|
I:GLY11
|
4.6
|
60.0
|
1.0
|
C
|
I:GLY128
|
4.7
|
56.1
|
1.0
|
O2B
|
I:ADP301
|
4.8
|
67.7
|
1.0
|
CA
|
J:GLY11
|
4.8
|
53.6
|
1.0
|
CA
|
I:LEU127
|
4.8
|
46.7
|
1.0
|
O3A
|
I:ADP301
|
4.9
|
61.0
|
1.0
|
OD1
|
J:ASP129
|
4.9
|
73.2
|
1.0
|
CG
|
J:ASP129
|
4.9
|
75.9
|
1.0
|
|
Fluorine binding site 9 out
of 12 in 8oie
Go back to
Fluorine Binding Sites List in 8oie
Fluorine binding site 9 out
of 12 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 9 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:F303
b:71.1
occ:1.00
|
F3
|
I:AF3303
|
0.0
|
71.1
|
1.0
|
AL
|
I:AF3303
|
1.8
|
61.5
|
1.0
|
O1B
|
I:ADP301
|
2.5
|
68.6
|
1.0
|
NZ
|
I:LYS42
|
2.8
|
62.9
|
1.0
|
NZ
|
J:LYS10
|
3.0
|
56.4
|
1.0
|
F2
|
I:AF3303
|
3.1
|
70.9
|
1.0
|
F1
|
I:AF3303
|
3.1
|
76.6
|
1.0
|
CE
|
J:LYS10
|
3.7
|
58.8
|
1.0
|
CE
|
I:LYS42
|
3.9
|
62.5
|
1.0
|
PB
|
I:ADP301
|
4.0
|
54.2
|
1.0
|
OD1
|
J:ASP129
|
4.2
|
73.2
|
1.0
|
OD2
|
I:ASP40
|
4.2
|
72.5
|
1.0
|
CG
|
J:LYS10
|
4.2
|
63.1
|
1.0
|
N
|
I:GLY12
|
4.3
|
49.3
|
1.0
|
MG
|
I:MG302
|
4.5
|
56.1
|
1.0
|
O3A
|
I:ADP301
|
4.6
|
61.0
|
1.0
|
O2B
|
I:ADP301
|
4.6
|
67.7
|
1.0
|
CD
|
J:LYS10
|
4.6
|
58.7
|
1.0
|
CA
|
I:GLY12
|
4.7
|
50.7
|
1.0
|
N
|
J:GLY11
|
4.7
|
58.1
|
1.0
|
OD2
|
J:ASP129
|
4.8
|
77.7
|
1.0
|
O3B
|
I:ADP301
|
4.9
|
48.2
|
1.0
|
CG
|
J:ASP129
|
4.9
|
75.9
|
1.0
|
OD2
|
I:ASP44
|
4.9
|
72.7
|
1.0
|
|
Fluorine binding site 10 out
of 12 in 8oie
Go back to
Fluorine Binding Sites List in 8oie
Fluorine binding site 10 out
of 12 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 10 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:F303
b:74.1
occ:1.00
|
F1
|
J:AF3303
|
0.0
|
74.1
|
1.0
|
AL
|
J:AF3303
|
1.8
|
61.6
|
1.0
|
MG
|
J:MG302
|
2.1
|
61.2
|
1.0
|
O3B
|
J:ADP301
|
2.8
|
60.9
|
1.0
|
OD2
|
J:ASP40
|
3.0
|
77.9
|
1.0
|
F3
|
J:AF3303
|
3.1
|
68.3
|
1.0
|
F2
|
J:AF3303
|
3.1
|
80.0
|
1.0
|
O2B
|
J:ADP301
|
3.2
|
70.3
|
1.0
|
PB
|
J:ADP301
|
3.5
|
63.2
|
1.0
|
CA
|
J:LEU127
|
3.8
|
53.8
|
1.0
|
NZ
|
J:LYS42
|
4.0
|
69.4
|
1.0
|
CG
|
J:ASP40
|
4.0
|
71.3
|
1.0
|
OG
|
J:SER16
|
4.2
|
65.9
|
1.0
|
O1B
|
J:ADP301
|
4.3
|
61.9
|
1.0
|
CE
|
J:LYS15
|
4.3
|
52.0
|
1.0
|
CB
|
J:LEU127
|
4.4
|
51.5
|
1.0
|
O
|
J:VAL126
|
4.5
|
69.7
|
1.0
|
C
|
J:LEU127
|
4.6
|
53.9
|
1.0
|
N
|
J:GLY128
|
4.6
|
52.2
|
1.0
|
N
|
J:LEU127
|
4.6
|
56.9
|
1.0
|
NZ
|
J:LYS15
|
4.6
|
45.2
|
1.0
|
CB
|
J:ASP40
|
4.7
|
62.2
|
1.0
|
OD1
|
J:ASP44
|
4.8
|
84.4
|
1.0
|
C
|
J:VAL126
|
4.9
|
56.5
|
1.0
|
O3A
|
J:ADP301
|
4.9
|
62.9
|
1.0
|
OD1
|
J:ASP40
|
4.9
|
71.2
|
1.0
|
|
Reference:
F.V.Schmidt,
L.Schulz,
J.Zarzycki,
S.Prinz,
N.N.Oehlmann,
T.J.Erb,
J.G.Rebelein.
Structural Insights Into the Iron Nitrogenase Complex Nat.Struct.Mol.Biol. 2023.
ISSN: ESSN 1545-9985
DOI: 10.1038/S41594-023-01124-2
Page generated: Fri Aug 2 21:10:05 2024
|