Aluminium in PDB 1n2c: Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Enzymatic activity of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
All present enzymatic activity of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate:
1.18.6.1;
Protein crystallography data
The structure of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate, PDB code: 1n2c
was solved by
H.Schindelin,
C.Kisker,
D.C.Rees,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
3.00
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
79.000,
299.700,
334.500,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.8 /
23.8
|
Other elements in 1n2c:
The structure of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate also contains other interesting chemical elements:
Aluminium Binding Sites:
The binding sites of Aluminium atom in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
(pdb code 1n2c). This binding sites where shown within
5.0 Angstroms radius around Aluminium atom.
In total 4 binding sites of Aluminium where determined in the
Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate, PDB code: 1n2c:
Jump to Aluminium binding site number:
1;
2;
3;
4;
Aluminium binding site 1 out
of 4 in 1n2c
Go back to
Aluminium Binding Sites List in 1n2c
Aluminium binding site 1 out
of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Aluminium with other atoms in the Al binding
site number 1 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Al293
b:24.0
occ:1.00
|
AL
|
E:ALF293
|
0.0
|
24.0
|
1.0
|
F2
|
E:ALF293
|
1.8
|
24.0
|
1.0
|
F3
|
E:ALF293
|
1.8
|
24.0
|
1.0
|
F1
|
E:ALF293
|
1.8
|
24.0
|
1.0
|
F4
|
E:ALF293
|
1.8
|
24.0
|
1.0
|
O1B
|
E:ADP291
|
1.9
|
24.0
|
1.0
|
PB
|
E:ADP291
|
2.9
|
24.0
|
1.0
|
O3B
|
E:ADP291
|
3.1
|
24.0
|
1.0
|
MG
|
E:MG292
|
3.3
|
24.0
|
1.0
|
NZ
|
F:LYS10
|
3.5
|
13.4
|
1.0
|
O2B
|
E:ADP291
|
3.7
|
24.0
|
1.0
|
OD2
|
E:ASP39
|
3.7
|
10.8
|
1.0
|
N
|
E:GLY128
|
3.9
|
19.5
|
1.0
|
N
|
E:GLY12
|
3.9
|
2.0
|
1.0
|
NZ
|
E:LYS15
|
4.1
|
22.1
|
1.0
|
O3A
|
E:ADP291
|
4.2
|
24.0
|
1.0
|
OG
|
E:SER16
|
4.2
|
17.4
|
1.0
|
CA
|
E:GLY12
|
4.5
|
2.0
|
1.0
|
CE
|
F:LYS10
|
4.5
|
13.4
|
1.0
|
CG
|
E:LYS15
|
4.6
|
22.1
|
1.0
|
CA
|
E:GLY128
|
4.6
|
19.5
|
1.0
|
CA
|
E:LEU127
|
4.6
|
16.5
|
1.0
|
CD
|
E:LYS15
|
4.6
|
22.1
|
1.0
|
C
|
E:LEU127
|
4.7
|
16.5
|
1.0
|
OD1
|
F:ASP129
|
4.8
|
37.7
|
1.0
|
OD2
|
F:ASP129
|
4.9
|
37.7
|
1.0
|
NZ
|
E:LYS41
|
4.9
|
16.8
|
1.0
|
CG
|
E:ASP39
|
4.9
|
10.8
|
1.0
|
C
|
E:GLY11
|
4.9
|
29.9
|
1.0
|
O2A
|
E:ADP291
|
4.9
|
24.0
|
1.0
|
CE
|
E:LYS15
|
5.0
|
22.1
|
1.0
|
CA
|
E:GLY11
|
5.0
|
29.9
|
1.0
|
|
Aluminium binding site 2 out
of 4 in 1n2c
Go back to
Aluminium Binding Sites List in 1n2c
Aluminium binding site 2 out
of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Aluminium with other atoms in the Al binding
site number 2 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Al293
b:24.0
occ:1.00
|
AL
|
F:ALF293
|
0.0
|
24.0
|
1.0
|
F3
|
F:ALF293
|
1.8
|
24.0
|
1.0
|
F2
|
F:ALF293
|
1.8
|
24.0
|
1.0
|
F1
|
F:ALF293
|
1.8
|
24.0
|
1.0
|
F4
|
F:ALF293
|
1.8
|
24.0
|
1.0
|
O1B
|
F:ADP291
|
1.9
|
24.0
|
1.0
|
PB
|
F:ADP291
|
2.9
|
24.0
|
1.0
|
O3B
|
F:ADP291
|
3.1
|
24.0
|
1.0
|
MG
|
F:MG292
|
3.4
|
24.0
|
1.0
|
NZ
|
E:LYS10
|
3.4
|
21.1
|
1.0
|
O2B
|
F:ADP291
|
3.7
|
24.0
|
1.0
|
OD2
|
F:ASP39
|
3.7
|
19.8
|
1.0
|
N
|
F:GLY128
|
3.9
|
44.3
|
1.0
|
N
|
F:GLY12
|
3.9
|
24.7
|
1.0
|
NZ
|
F:LYS15
|
4.1
|
32.0
|
1.0
|
O3A
|
F:ADP291
|
4.2
|
24.0
|
1.0
|
OG
|
F:SER16
|
4.2
|
21.4
|
1.0
|
CE
|
E:LYS10
|
4.4
|
21.1
|
1.0
|
CA
|
F:GLY12
|
4.5
|
24.7
|
1.0
|
CG
|
F:LYS15
|
4.6
|
32.0
|
1.0
|
CA
|
F:GLY128
|
4.6
|
44.3
|
1.0
|
CA
|
F:LEU127
|
4.6
|
14.7
|
1.0
|
CD
|
F:LYS15
|
4.6
|
32.0
|
1.0
|
C
|
F:LEU127
|
4.7
|
14.7
|
1.0
|
OD1
|
E:ASP129
|
4.9
|
22.6
|
1.0
|
CG
|
F:ASP39
|
4.9
|
19.8
|
1.0
|
NZ
|
F:LYS41
|
4.9
|
29.7
|
1.0
|
OD2
|
E:ASP129
|
4.9
|
22.6
|
1.0
|
C
|
F:GLY11
|
4.9
|
5.3
|
1.0
|
O2A
|
F:ADP291
|
4.9
|
24.0
|
1.0
|
CE
|
F:LYS15
|
5.0
|
32.0
|
1.0
|
CA
|
F:GLY11
|
5.0
|
5.3
|
1.0
|
|
Aluminium binding site 3 out
of 4 in 1n2c
Go back to
Aluminium Binding Sites List in 1n2c
Aluminium binding site 3 out
of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Aluminium with other atoms in the Al binding
site number 3 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Al293
b:24.0
occ:1.00
|
AL
|
G:ALF293
|
0.0
|
24.0
|
1.0
|
F3
|
G:ALF293
|
1.8
|
24.0
|
1.0
|
F2
|
G:ALF293
|
1.8
|
24.0
|
1.0
|
F1
|
G:ALF293
|
1.8
|
24.0
|
1.0
|
O1B
|
G:ADP291
|
1.8
|
24.0
|
1.0
|
F4
|
G:ALF293
|
1.8
|
24.0
|
1.0
|
PB
|
G:ADP291
|
2.9
|
24.0
|
1.0
|
O3B
|
G:ADP291
|
3.1
|
24.0
|
1.0
|
MG
|
G:MG292
|
3.4
|
24.0
|
1.0
|
NZ
|
H:LYS10
|
3.5
|
10.4
|
1.0
|
O2B
|
G:ADP291
|
3.7
|
24.0
|
1.0
|
OD2
|
G:ASP39
|
3.7
|
13.3
|
1.0
|
N
|
G:GLY12
|
3.9
|
22.7
|
1.0
|
N
|
G:GLY128
|
3.9
|
16.3
|
1.0
|
NZ
|
G:LYS15
|
4.1
|
32.1
|
1.0
|
O3A
|
G:ADP291
|
4.1
|
24.0
|
1.0
|
OG
|
G:SER16
|
4.2
|
7.2
|
1.0
|
CA
|
G:GLY12
|
4.4
|
22.7
|
1.0
|
CE
|
H:LYS10
|
4.5
|
10.4
|
1.0
|
CG
|
G:LYS15
|
4.6
|
32.1
|
1.0
|
CA
|
G:GLY128
|
4.6
|
16.3
|
1.0
|
CD
|
G:LYS15
|
4.6
|
32.1
|
1.0
|
CA
|
G:LEU127
|
4.6
|
12.2
|
1.0
|
C
|
G:LEU127
|
4.7
|
12.2
|
1.0
|
OD1
|
H:ASP129
|
4.7
|
31.6
|
1.0
|
OD2
|
H:ASP129
|
4.8
|
31.6
|
1.0
|
C
|
G:GLY11
|
4.9
|
38.0
|
1.0
|
NZ
|
G:LYS41
|
4.9
|
32.0
|
1.0
|
CG
|
G:ASP39
|
4.9
|
13.3
|
1.0
|
O2A
|
G:ADP291
|
4.9
|
24.0
|
1.0
|
CE
|
G:LYS15
|
5.0
|
32.1
|
1.0
|
CA
|
G:GLY11
|
5.0
|
38.0
|
1.0
|
|
Aluminium binding site 4 out
of 4 in 1n2c
Go back to
Aluminium Binding Sites List in 1n2c
Aluminium binding site 4 out
of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Aluminium with other atoms in the Al binding
site number 4 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Al293
b:24.0
occ:1.00
|
AL
|
H:ALF293
|
0.0
|
24.0
|
1.0
|
F2
|
H:ALF293
|
1.8
|
24.0
|
1.0
|
F3
|
H:ALF293
|
1.8
|
24.0
|
1.0
|
F1
|
H:ALF293
|
1.8
|
24.0
|
1.0
|
F4
|
H:ALF293
|
1.8
|
24.0
|
1.0
|
O1B
|
H:ADP291
|
1.9
|
24.0
|
1.0
|
PB
|
H:ADP291
|
3.0
|
24.0
|
1.0
|
O3B
|
H:ADP291
|
3.1
|
24.0
|
1.0
|
MG
|
H:MG292
|
3.3
|
24.0
|
1.0
|
NZ
|
G:LYS10
|
3.4
|
25.2
|
1.0
|
O2B
|
H:ADP291
|
3.7
|
24.0
|
1.0
|
OD2
|
H:ASP39
|
3.7
|
15.3
|
1.0
|
N
|
H:GLY128
|
3.9
|
34.0
|
1.0
|
N
|
H:GLY12
|
3.9
|
28.5
|
1.0
|
NZ
|
H:LYS15
|
4.1
|
27.1
|
1.0
|
O3A
|
H:ADP291
|
4.2
|
24.0
|
1.0
|
OG
|
H:SER16
|
4.2
|
22.9
|
1.0
|
CE
|
G:LYS10
|
4.3
|
25.2
|
1.0
|
CA
|
H:GLY12
|
4.5
|
28.5
|
1.0
|
CG
|
H:LYS15
|
4.6
|
27.1
|
1.0
|
CA
|
H:GLY128
|
4.6
|
34.0
|
1.0
|
CA
|
H:LEU127
|
4.6
|
28.5
|
1.0
|
CD
|
H:LYS15
|
4.6
|
27.1
|
1.0
|
C
|
H:LEU127
|
4.7
|
28.5
|
1.0
|
CG
|
H:ASP39
|
4.9
|
15.3
|
1.0
|
NZ
|
H:LYS41
|
4.9
|
23.2
|
1.0
|
C
|
H:GLY11
|
4.9
|
21.9
|
1.0
|
O2A
|
H:ADP291
|
4.9
|
24.0
|
1.0
|
OD1
|
G:ASP129
|
5.0
|
31.2
|
1.0
|
CE
|
H:LYS15
|
5.0
|
27.1
|
1.0
|
CA
|
H:GLY11
|
5.0
|
21.9
|
1.0
|
OD2
|
G:ASP129
|
5.0
|
31.2
|
1.0
|
|
Reference:
H.Schindelin,
C.Kisker,
J.L.Schlessman,
J.B.Howard,
D.C.Rees.
Structure of Adp X AIF4(-)-Stabilized Nitrogenase Complex and Its Implications For Signal Transduction. Nature V. 387 370 1997.
ISSN: ISSN 0028-0836
PubMed: 9163420
DOI: 10.1038/387370A0
Page generated: Wed Jul 10 09:24:16 2024
|