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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:

Fluorine (F) 16 atoms
Molybdenum (Mo) 2 atoms
Magnesium (Mg) 4 atoms
Aluminium (Al) 4 atoms
Calcium (Ca) 2 atoms

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

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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

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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

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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

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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

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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

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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

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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

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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

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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

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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: Sun Dec 13 14:24:49 2020

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