Iron 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:
Iron Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
30;
Page 4, Binding sites: 31 -
38;
Binding sites:
The binding sites of Iron 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 Iron atom.
In total 38 binding sites of Iron where determined in the
Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate, PDB code: 1n2c:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 38 in 1n2c
Go back to
Iron Binding Sites List in 1n2c
Iron binding site 1 out
of 38 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe 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
|
A:Fe496
b:24.0
occ:1.00
|
FE1
|
A:CFM496
|
0.0
|
24.0
|
1.0
|
S2A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
S4A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
SG
|
A:CYS275
|
2.3
|
18.8
|
1.0
|
S1A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
FE3
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
FE4
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
FE2
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
CB
|
A:CYS275
|
3.4
|
18.8
|
1.0
|
OG
|
A:SER278
|
3.6
|
32.5
|
1.0
|
CB
|
A:LEU358
|
4.2
|
21.9
|
1.0
|
CE2
|
A:TYR229
|
4.3
|
22.4
|
1.0
|
CB
|
A:SER278
|
4.4
|
32.5
|
1.0
|
CA
|
A:CYS275
|
4.5
|
18.8
|
1.0
|
CD2
|
A:LEU358
|
4.6
|
21.9
|
1.0
|
S5
|
A:CFM496
|
4.7
|
24.0
|
1.0
|
FE5
|
A:CFM496
|
4.7
|
24.0
|
1.0
|
S3A
|
A:CFM496
|
4.8
|
24.0
|
1.0
|
S2B
|
A:CFM496
|
4.8
|
24.0
|
1.0
|
FE7
|
A:CFM496
|
4.8
|
24.0
|
1.0
|
FE6
|
A:CFM496
|
4.9
|
24.0
|
1.0
|
CD2
|
A:TYR229
|
4.9
|
22.4
|
1.0
|
|
Iron binding site 2 out
of 38 in 1n2c
Go back to
Iron Binding Sites List in 1n2c
Iron binding site 2 out
of 38 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe 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
|
A:Fe496
b:24.0
occ:1.00
|
FE2
|
A:CFM496
|
0.0
|
24.0
|
1.0
|
S2B
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
S2A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
S1A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
FE6
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
FE3
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
FE4
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
FE1
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
FE5
|
A:CFM496
|
3.4
|
24.0
|
1.0
|
FE7
|
A:CFM496
|
3.5
|
24.0
|
1.0
|
CZ
|
A:PHE381
|
3.7
|
33.4
|
1.0
|
S4A
|
A:CFM496
|
3.9
|
24.0
|
1.0
|
S1B
|
A:CFM496
|
4.1
|
24.0
|
1.0
|
CE1
|
A:HIS195
|
4.1
|
30.6
|
1.0
|
CE1
|
A:PHE381
|
4.2
|
33.4
|
1.0
|
S3B
|
A:CFM496
|
4.2
|
24.0
|
1.0
|
NE2
|
A:HIS195
|
4.3
|
30.6
|
1.0
|
S3A
|
A:CFM496
|
4.4
|
24.0
|
1.0
|
S5
|
A:CFM496
|
4.5
|
24.0
|
1.0
|
NH2
|
A:ARG96
|
4.6
|
19.5
|
1.0
|
SG
|
A:CYS275
|
4.7
|
18.8
|
1.0
|
CG1
|
A:VAL70
|
4.8
|
33.6
|
1.0
|
N
|
A:GLY357
|
4.8
|
16.0
|
1.0
|
MO1
|
A:CFM496
|
4.8
|
24.0
|
1.0
|
CE2
|
A:PHE381
|
4.9
|
33.4
|
1.0
|
|
Iron binding site 3 out
of 38 in 1n2c
Go back to
Iron Binding Sites List in 1n2c
Iron binding site 3 out
of 38 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe 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
|
A:Fe496
b:24.0
occ:1.00
|
FE3
|
A:CFM496
|
0.0
|
24.0
|
1.0
|
S2A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
S5
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
S4A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
FE7
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
FE1
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
FE2
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
FE4
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
FE5
|
A:CFM496
|
3.5
|
24.0
|
1.0
|
NH2
|
A:ARG96
|
3.5
|
19.5
|
1.0
|
FE6
|
A:CFM496
|
3.6
|
24.0
|
1.0
|
S1A
|
A:CFM496
|
3.8
|
24.0
|
1.0
|
CD2
|
A:TYR229
|
3.9
|
22.4
|
1.0
|
CE2
|
A:TYR229
|
4.0
|
22.4
|
1.0
|
S4B
|
A:CFM496
|
4.2
|
24.0
|
1.0
|
S3B
|
A:CFM496
|
4.3
|
24.0
|
1.0
|
S3A
|
A:CFM496
|
4.5
|
24.0
|
1.0
|
S2B
|
A:CFM496
|
4.5
|
24.0
|
1.0
|
SG
|
A:CYS275
|
4.6
|
18.8
|
1.0
|
CZ
|
A:ARG96
|
4.8
|
19.5
|
1.0
|
MO1
|
A:CFM496
|
5.0
|
24.0
|
1.0
|
CG
|
A:TYR229
|
5.0
|
22.4
|
1.0
|
NE
|
A:ARG359
|
5.0
|
22.2
|
1.0
|
|
Iron binding site 4 out
of 38 in 1n2c
Go back to
Iron Binding Sites List in 1n2c
Iron binding site 4 out
of 38 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe 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
|
A:Fe496
b:24.0
occ:1.00
|
FE4
|
A:CFM496
|
0.0
|
24.0
|
1.0
|
S3A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
S1A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
S4A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
FE5
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
FE1
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
FE3
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
FE2
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
FE7
|
A:CFM496
|
3.6
|
24.0
|
1.0
|
FE6
|
A:CFM496
|
3.7
|
24.0
|
1.0
|
N
|
A:GLY357
|
3.8
|
16.0
|
1.0
|
S2A
|
A:CFM496
|
3.9
|
24.0
|
1.0
|
CB
|
A:LEU358
|
4.2
|
21.9
|
1.0
|
S4B
|
A:CFM496
|
4.2
|
24.0
|
1.0
|
N
|
A:LEU358
|
4.3
|
21.9
|
1.0
|
S1B
|
A:CFM496
|
4.3
|
24.0
|
1.0
|
CA
|
A:GLY356
|
4.4
|
26.3
|
1.0
|
S5
|
A:CFM496
|
4.5
|
24.0
|
1.0
|
C
|
A:GLY357
|
4.5
|
16.0
|
1.0
|
CG
|
A:ARG359
|
4.6
|
22.2
|
1.0
|
S2B
|
A:CFM496
|
4.6
|
24.0
|
1.0
|
N
|
A:ARG359
|
4.6
|
22.2
|
1.0
|
SG
|
A:CYS275
|
4.6
|
18.8
|
1.0
|
C
|
A:GLY356
|
4.6
|
26.3
|
1.0
|
CA
|
A:GLY357
|
4.7
|
16.0
|
1.0
|
CA
|
A:LEU358
|
4.8
|
21.9
|
1.0
|
CD
|
A:ARG359
|
4.8
|
22.2
|
1.0
|
CZ
|
A:PHE381
|
4.8
|
33.4
|
1.0
|
N
|
A:GLY356
|
4.8
|
26.3
|
1.0
|
NE
|
A:ARG359
|
4.9
|
22.2
|
1.0
|
MO1
|
A:CFM496
|
5.0
|
24.0
|
1.0
|
|
Iron binding site 5 out
of 38 in 1n2c
Go back to
Iron Binding Sites List in 1n2c
Iron binding site 5 out
of 38 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe496
b:24.0
occ:1.00
|
FE5
|
A:CFM496
|
0.0
|
24.0
|
1.0
|
S3A
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
S4B
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
S1B
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
FE4
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
FE7
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
FE6
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
MO1
|
A:CFM496
|
2.7
|
24.0
|
1.0
|
FE2
|
A:CFM496
|
3.4
|
24.0
|
1.0
|
FE3
|
A:CFM496
|
3.5
|
24.0
|
1.0
|
ND1
|
A:HIS442
|
3.6
|
19.5
|
1.0
|
S3B
|
A:CFM496
|
3.8
|
24.0
|
1.0
|
CA
|
A:GLY356
|
3.9
|
26.3
|
1.0
|
N
|
A:GLY356
|
3.9
|
26.3
|
1.0
|
CE1
|
A:HIS442
|
4.0
|
19.5
|
1.0
|
S1A
|
A:CFM496
|
4.1
|
24.0
|
1.0
|
CG2
|
A:ILE355
|
4.2
|
19.1
|
1.0
|
S4A
|
A:CFM496
|
4.2
|
24.0
|
1.0
|
S2B
|
A:CFM496
|
4.4
|
24.0
|
1.0
|
S5
|
A:CFM496
|
4.4
|
24.0
|
1.0
|
O7
|
A:HCA494
|
4.5
|
24.0
|
1.0
|
O5
|
A:HCA494
|
4.6
|
24.0
|
1.0
|
CD
|
A:ARG359
|
4.6
|
22.2
|
1.0
|
N
|
A:GLY357
|
4.7
|
16.0
|
1.0
|
FE1
|
A:CFM496
|
4.7
|
24.0
|
1.0
|
CG
|
A:HIS442
|
4.7
|
19.5
|
1.0
|
CZ
|
A:PHE381
|
4.9
|
33.4
|
1.0
|
C
|
A:GLY356
|
4.9
|
26.3
|
1.0
|
NE
|
A:ARG359
|
4.9
|
22.2
|
1.0
|
|
Iron binding site 6 out
of 38 in 1n2c
Go back to
Iron Binding Sites List in 1n2c
Iron binding site 6 out
of 38 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe496
b:24.0
occ:1.00
|
FE6
|
A:CFM496
|
0.0
|
24.0
|
1.0
|
S1B
|
A:CFM496
|
2.2
|
24.0
|
1.0
|
S2B
|
A:CFM496
|
2.2
|
24.0
|
1.0
|
S3B
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
FE2
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
FE5
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
MO1
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
FE7
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
O7
|
A:HCA494
|
3.6
|
24.0
|
1.0
|
FE3
|
A:CFM496
|
3.6
|
24.0
|
1.0
|
FE4
|
A:CFM496
|
3.7
|
24.0
|
1.0
|
S4B
|
A:CFM496
|
3.8
|
24.0
|
1.0
|
CZ
|
A:PHE381
|
4.0
|
33.4
|
1.0
|
CG1
|
A:VAL70
|
4.1
|
33.6
|
1.0
|
S2A
|
A:CFM496
|
4.2
|
24.0
|
1.0
|
O1
|
A:HCA494
|
4.3
|
24.0
|
1.0
|
S1A
|
A:CFM496
|
4.3
|
24.0
|
1.0
|
O5
|
A:HCA494
|
4.3
|
24.0
|
1.0
|
CE2
|
A:PHE381
|
4.5
|
33.4
|
1.0
|
S3A
|
A:CFM496
|
4.5
|
24.0
|
1.0
|
ND1
|
A:HIS442
|
4.5
|
19.5
|
1.0
|
S5
|
A:CFM496
|
4.6
|
24.0
|
1.0
|
NH2
|
A:ARG96
|
4.6
|
19.5
|
1.0
|
C3
|
A:HCA494
|
4.7
|
24.0
|
1.0
|
CA
|
A:GLY356
|
4.8
|
26.3
|
1.0
|
CE1
|
A:HIS442
|
4.8
|
19.5
|
1.0
|
FE1
|
A:CFM496
|
4.9
|
24.0
|
1.0
|
C2
|
A:HCA494
|
5.0
|
24.0
|
1.0
|
|
Iron binding site 7 out
of 38 in 1n2c
Go back to
Iron Binding Sites List in 1n2c
Iron binding site 7 out
of 38 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe496
b:24.0
occ:1.00
|
FE7
|
A:CFM496
|
0.0
|
24.0
|
1.0
|
S4B
|
A:CFM496
|
2.2
|
24.0
|
1.0
|
S5
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
S3B
|
A:CFM496
|
2.3
|
24.0
|
1.0
|
FE5
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
FE3
|
A:CFM496
|
2.5
|
24.0
|
1.0
|
FE6
|
A:CFM496
|
2.6
|
24.0
|
1.0
|
MO1
|
A:CFM496
|
2.7
|
24.0
|
1.0
|
NH2
|
A:ARG96
|
3.5
|
19.5
|
1.0
|
FE2
|
A:CFM496
|
3.5
|
24.0
|
1.0
|
O5
|
A:HCA494
|
3.6
|
24.0
|
1.0
|
FE4
|
A:CFM496
|
3.6
|
24.0
|
1.0
|
S1B
|
A:CFM496
|
3.9
|
24.0
|
1.0
|
CD1
|
A:ILE231
|
3.9
|
20.1
|
1.0
|
NE
|
A:ARG96
|
4.1
|
19.5
|
1.0
|
S2A
|
A:CFM496
|
4.2
|
24.0
|
1.0
|
CZ
|
A:ARG96
|
4.2
|
19.5
|
1.0
|
S4A
|
A:CFM496
|
4.2
|
24.0
|
1.0
|
S3A
|
A:CFM496
|
4.5
|
24.0
|
1.0
|
S2B
|
A:CFM496
|
4.5
|
24.0
|
1.0
|
O7
|
A:HCA494
|
4.6
|
24.0
|
1.0
|
CZ
|
A:ARG359
|
4.6
|
22.2
|
1.0
|
ND1
|
A:HIS442
|
4.6
|
19.5
|
1.0
|
NH1
|
A:ARG359
|
4.7
|
22.2
|
1.0
|
NH2
|
A:ARG359
|
4.8
|
22.2
|
1.0
|
FE1
|
A:CFM496
|
4.8
|
24.0
|
1.0
|
C7
|
A:HCA494
|
4.9
|
24.0
|
1.0
|
NE
|
A:ARG359
|
4.9
|
22.2
|
1.0
|
|
Iron binding site 8 out
of 38 in 1n2c
Go back to
Iron Binding Sites List in 1n2c
Iron binding site 8 out
of 38 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe525
b:24.0
occ:1.00
|
FE1
|
B:CLF525
|
0.0
|
24.0
|
1.0
|
S1
|
B:CLF525
|
2.3
|
24.0
|
1.0
|
SG
|
B:CYS95
|
2.3
|
3.2
|
1.0
|
S3A
|
B:CLF525
|
2.3
|
24.0
|
1.0
|
S2A
|
B:CLF525
|
2.3
|
24.0
|
1.0
|
FE2
|
B:CLF525
|
2.6
|
24.0
|
1.0
|
FE4
|
B:CLF525
|
2.6
|
24.0
|
1.0
|
FE3
|
B:CLF525
|
2.7
|
24.0
|
1.0
|
FE8
|
B:CLF525
|
2.9
|
24.0
|
1.0
|
N
|
B:CYS95
|
3.4
|
3.2
|
1.0
|
CB
|
B:CYS95
|
3.6
|
3.2
|
1.0
|
CA
|
B:CYS95
|
3.7
|
3.2
|
1.0
|
S4A
|
B:CLF525
|
3.8
|
24.0
|
1.0
|
S4B
|
B:CLF525
|
3.8
|
24.0
|
1.0
|
C
|
B:GLY94
|
4.1
|
5.8
|
1.0
|
FE5
|
B:CLF525
|
4.2
|
24.0
|
1.0
|
SG
|
A:CYS154
|
4.3
|
14.8
|
1.0
|
CB
|
B:SER92
|
4.4
|
30.8
|
1.0
|
SG
|
A:CYS88
|
4.4
|
9.9
|
1.0
|
CA
|
B:GLY94
|
4.5
|
5.8
|
1.0
|
CG2
|
B:THR152
|
4.5
|
21.8
|
1.0
|
SG
|
A:CYS62
|
4.7
|
21.0
|
1.0
|
O
|
B:GLY94
|
4.8
|
5.8
|
1.0
|
FE6
|
B:CLF525
|
4.9
|
24.0
|
1.0
|
O
|
B:SER92
|
4.9
|
30.8
|
1.0
|
N
|
B:GLY94
|
4.9
|
5.8
|
1.0
|
|
Iron binding site 9 out
of 38 in 1n2c
Go back to
Iron Binding Sites List in 1n2c
Iron binding site 9 out
of 38 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe525
b:24.0
occ:1.00
|
FE2
|
B:CLF525
|
0.0
|
24.0
|
1.0
|
S2A
|
B:CLF525
|
2.3
|
24.0
|
1.0
|
SG
|
A:CYS154
|
2.3
|
14.8
|
1.0
|
S4A
|
B:CLF525
|
2.3
|
24.0
|
1.0
|
S1
|
B:CLF525
|
2.3
|
24.0
|
1.0
|
FE1
|
B:CLF525
|
2.6
|
24.0
|
1.0
|
FE3
|
B:CLF525
|
2.7
|
24.0
|
1.0
|
FE4
|
B:CLF525
|
2.7
|
24.0
|
1.0
|
CA
|
A:GLY185
|
3.3
|
21.3
|
1.0
|
N
|
A:GLY185
|
3.7
|
21.3
|
1.0
|
CB
|
A:CYS154
|
3.7
|
14.8
|
1.0
|
N
|
A:CYS154
|
3.8
|
14.8
|
1.0
|
S3A
|
B:CLF525
|
3.9
|
24.0
|
1.0
|
CB
|
B:SER92
|
4.1
|
30.8
|
1.0
|
OG
|
B:SER92
|
4.1
|
30.8
|
1.0
|
C
|
A:GLY185
|
4.2
|
21.3
|
1.0
|
CA
|
A:CYS154
|
4.3
|
14.8
|
1.0
|
N
|
A:PHE186
|
4.5
|
20.6
|
1.0
|
SG
|
B:CYS95
|
4.5
|
3.2
|
1.0
|
SG
|
A:CYS62
|
4.6
|
21.0
|
1.0
|
FE8
|
B:CLF525
|
4.6
|
24.0
|
1.0
|
CB
|
A:CYS62
|
4.7
|
21.0
|
1.0
|
C
|
A:GLU153
|
4.9
|
13.2
|
1.0
|
SG
|
A:CYS88
|
4.9
|
9.9
|
1.0
|
CG2
|
B:THR152
|
5.0
|
21.8
|
1.0
|
|
Iron binding site 10 out
of 38 in 1n2c
Go back to
Iron Binding Sites List in 1n2c
Iron binding site 10 out
of 38 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe525
b:24.0
occ:1.00
|
FE3
|
B:CLF525
|
0.0
|
24.0
|
1.0
|
S4A
|
B:CLF525
|
2.3
|
24.0
|
1.0
|
S2A
|
B:CLF525
|
2.3
|
24.0
|
1.0
|
SG
|
A:CYS62
|
2.3
|
21.0
|
1.0
|
S3A
|
B:CLF525
|
2.3
|
24.0
|
1.0
|
FE4
|
B:CLF525
|
2.5
|
24.0
|
1.0
|
FE1
|
B:CLF525
|
2.7
|
24.0
|
1.0
|
FE2
|
B:CLF525
|
2.7
|
24.0
|
1.0
|
CB
|
A:CYS62
|
3.2
|
21.0
|
1.0
|
CA
|
A:GLY185
|
3.9
|
21.3
|
1.0
|
S1
|
B:CLF525
|
3.9
|
24.0
|
1.0
|
CB
|
A:TYR64
|
3.9
|
17.6
|
1.0
|
CA
|
B:GLY94
|
4.3
|
5.8
|
1.0
|
SG
|
A:CYS88
|
4.4
|
9.9
|
1.0
|
C
|
B:GLY94
|
4.5
|
5.8
|
1.0
|
CG
|
A:TYR64
|
4.5
|
17.6
|
1.0
|
N
|
A:GLY185
|
4.6
|
21.3
|
1.0
|
CD2
|
A:TYR64
|
4.6
|
17.6
|
1.0
|
CE2
|
B:TYR98
|
4.6
|
14.9
|
1.0
|
N
|
B:CYS95
|
4.6
|
3.2
|
1.0
|
CA
|
A:CYS62
|
4.6
|
21.0
|
1.0
|
SG
|
B:CYS95
|
4.9
|
3.2
|
1.0
|
CD2
|
B:TYR98
|
4.9
|
14.9
|
1.0
|
SG
|
A:CYS154
|
4.9
|
14.8
|
1.0
|
N
|
A:TYR64
|
5.0
|
17.6
|
1.0
|
C
|
A:GLY185
|
5.0
|
21.3
|
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: Sat Aug 3 11:13:55 2024
|