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Iron in PDB 9cje: Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover

Enzymatic activity of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover

All present enzymatic activity of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover:
1.18.6.1;

Other elements in 9cje:

The structure of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover also contains other interesting chemical elements:

Molybdenum (Mo) 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 - 32;

Binding sites:

The binding sites of Iron atom in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover (pdb code 9cje). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 32 binding sites of Iron where determined in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover, PDB code: 9cje:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 32 in 9cje

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Iron binding site 1 out of 32 in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:43.7
occ:1.00
FE1 A:ICS501 0.0 43.7 1.0
SG A:CYS275 2.3 25.5 1.0
S2A A:ICS501 2.3 24.2 1.0
S4A A:ICS501 2.3 18.9 1.0
S1A A:ICS501 2.3 27.8 1.0
FE4 A:ICS501 2.6 39.8 1.0
FE3 A:ICS501 2.7 37.9 1.0
FE2 A:ICS501 2.7 39.2 1.0
CB A:CYS275 3.3 21.7 1.0
CX A:ICS501 3.4 30.4 1.0
CB A:LEU358 4.0 26.9 1.0
OG A:SER278 4.3 25.5 1.0
CB A:SER278 4.5 17.7 1.0
CA A:CYS275 4.5 26.0 1.0
CE2 A:TYR229 4.5 16.1 1.0
CD2 A:LEU358 4.5 25.7 1.0
N A:LEU358 4.7 21.6 1.0
S3A A:ICS501 4.8 29.0 1.0
S5A A:ICS501 4.8 26.6 1.0
S2B A:ICS501 4.8 22.7 1.0
CG A:LEU358 4.9 30.1 1.0
FE7 A:ICS501 5.0 37.3 1.0
FE5 A:ICS501 5.0 52.2 1.0

Iron binding site 2 out of 32 in 9cje

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Iron binding site 2 out of 32 in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:39.2
occ:1.00
FE2 A:ICS501 0.0 39.2 1.0
CX A:ICS501 2.0 30.4 1.0
S2B A:ICS501 2.2 22.7 1.0
S2A A:ICS501 2.2 24.2 1.0
S1A A:ICS501 2.3 27.8 1.0
FE6 A:ICS501 2.6 42.5 1.0
FE4 A:ICS501 2.7 39.8 1.0
FE1 A:ICS501 2.7 43.7 1.0
FE3 A:ICS501 2.7 37.9 1.0
FE5 A:ICS501 3.7 52.2 1.0
FE7 A:ICS501 3.7 37.3 1.0
S4A A:ICS501 3.9 18.9 1.0
CZ A:PHE381 3.9 22.3 1.0
CE1 A:HIS195 4.0 20.9 1.0
NE2 A:HIS195 4.1 22.1 1.0
S1B A:ICS501 4.2 33.8 1.0
S3B A:ICS501 4.2 17.7 1.0
CE1 A:PHE381 4.4 24.4 1.0
CG1 A:VAL70 4.4 16.1 1.0
S3A A:ICS501 4.5 29.0 1.0
S5A A:ICS501 4.5 26.6 1.0
SG A:CYS275 4.6 25.5 1.0
CG2 A:VAL70 4.8 24.6 1.0
N A:GLY357 4.9 25.8 1.0
CE2 A:PHE381 5.0 21.7 1.0

Iron binding site 3 out of 32 in 9cje

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Iron binding site 3 out of 32 in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:37.9
occ:1.00
FE3 A:ICS501 0.0 37.9 1.0
CX A:ICS501 2.0 30.4 1.0
S5A A:ICS501 2.2 26.6 1.0
S4A A:ICS501 2.3 18.9 1.0
S2A A:ICS501 2.3 24.2 1.0
FE7 A:ICS501 2.6 37.3 1.0
FE4 A:ICS501 2.6 39.8 1.0
FE1 A:ICS501 2.7 43.7 1.0
FE2 A:ICS501 2.7 39.2 1.0
FE6 A:ICS501 3.7 42.5 1.0
FE5 A:ICS501 3.7 52.2 1.0
NH2 A:ARG96 3.8 21.6 1.0
S1A A:ICS501 3.9 27.8 1.0
O A:HOH743 3.9 26.9 1.0
S4B A:ICS501 4.2 23.3 1.0
S3B A:ICS501 4.2 17.7 1.0
CD2 A:TYR229 4.3 19.9 1.0
S2B A:ICS501 4.4 22.7 1.0
CE2 A:TYR229 4.5 16.1 1.0
S3A A:ICS501 4.5 29.0 1.0
SG A:CYS275 4.8 25.5 1.0
NE A:ARG359 4.8 30.2 1.0
NH2 A:ARG359 4.9 20.3 1.0
CZ A:ARG96 4.9 13.2 1.0

Iron binding site 4 out of 32 in 9cje

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Iron binding site 4 out of 32 in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:39.8
occ:1.00
FE4 A:ICS501 0.0 39.8 1.0
CX A:ICS501 2.0 30.4 1.0
S3A A:ICS501 2.2 29.0 1.0
S4A A:ICS501 2.3 18.9 1.0
S1A A:ICS501 2.3 27.8 1.0
FE5 A:ICS501 2.6 52.2 1.0
FE1 A:ICS501 2.6 43.7 1.0
FE3 A:ICS501 2.6 37.9 1.0
FE2 A:ICS501 2.7 39.2 1.0
FE7 A:ICS501 3.7 37.3 1.0
N A:LEU358 3.7 21.6 1.0
FE6 A:ICS501 3.7 42.5 1.0
S2A A:ICS501 3.8 24.2 1.0
N A:GLY357 3.9 25.8 1.0
CB A:LEU358 4.1 26.9 1.0
S4B A:ICS501 4.2 23.3 1.0
S1B A:ICS501 4.3 33.8 1.0
CA A:LEU358 4.4 18.4 1.0
C A:GLY357 4.5 28.6 1.0
S5A A:ICS501 4.5 26.6 1.0
N A:ARG359 4.5 30.9 1.0
CA A:GLY357 4.5 25.2 1.0
S2B A:ICS501 4.5 22.7 1.0
SG A:CYS275 4.7 25.5 1.0
CG A:ARG359 4.7 22.4 1.0
CD A:ARG359 4.8 24.0 1.0
NE A:ARG359 4.8 30.2 1.0
CZ A:PHE381 4.9 22.3 1.0
C A:GLY356 5.0 23.8 1.0

Iron binding site 5 out of 32 in 9cje

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Iron binding site 5 out of 32 in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:52.2
occ:1.00
FE5 A:ICS501 0.0 52.2 1.0
CX A:ICS501 2.0 30.4 1.0
S4B A:ICS501 2.3 23.3 1.0
S3A A:ICS501 2.3 29.0 1.0
S1B A:ICS501 2.3 33.8 1.0
FE4 A:ICS501 2.6 39.8 1.0
FE7 A:ICS501 2.6 37.3 1.0
FE6 A:ICS501 2.6 42.5 1.0
MO1 A:ICS501 2.7 56.8 1.0
FE2 A:ICS501 3.7 39.2 1.0
FE3 A:ICS501 3.7 37.9 1.0
ND1 A:HIS442 3.8 31.2 1.0
S3B A:ICS501 3.9 17.7 1.0
CG2 A:ILE355 3.9 26.2 1.0
N A:GLY356 4.0 28.0 1.0
CE1 A:HIS442 4.0 27.9 1.0
CA A:GLY356 4.2 18.2 1.0
S1A A:ICS501 4.3 27.8 1.0
S4A A:ICS501 4.3 18.9 1.0
S2B A:ICS501 4.5 22.7 1.0
S5A A:ICS501 4.5 26.6 1.0
N A:GLY357 4.5 25.8 1.0
CD A:ARG359 4.6 24.0 1.0
O7 A:HCA502 4.6 30.6 1.0
CG A:HIS442 4.7 27.8 1.0
O5 A:HCA502 4.7 36.5 1.0
NE A:ARG359 4.8 30.2 1.0
C A:GLY356 4.9 23.8 1.0
NE2 A:HIS442 5.0 32.0 1.0
CZ A:PHE381 5.0 22.3 1.0
FE1 A:ICS501 5.0 43.7 1.0

Iron binding site 6 out of 32 in 9cje

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Iron binding site 6 out of 32 in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:42.5
occ:1.00
FE6 A:ICS501 0.0 42.5 1.0
CX A:ICS501 2.0 30.4 1.0
S2B A:ICS501 2.2 22.7 1.0
S3B A:ICS501 2.2 17.7 1.0
S1B A:ICS501 2.2 33.8 1.0
FE7 A:ICS501 2.6 37.3 1.0
FE2 A:ICS501 2.6 39.2 1.0
FE5 A:ICS501 2.6 52.2 1.0
MO1 A:ICS501 2.7 56.8 1.0
O7 A:HCA502 3.6 30.6 1.0
FE3 A:ICS501 3.7 37.9 1.0
FE4 A:ICS501 3.7 39.8 1.0
S4B A:ICS501 3.8 23.3 1.0
CZ A:PHE381 4.1 22.3 1.0
S2A A:ICS501 4.2 24.2 1.0
S1A A:ICS501 4.3 27.8 1.0
CG2 A:VAL70 4.4 24.6 1.0
O1 A:HCA502 4.4 32.5 1.0
S5A A:ICS501 4.4 26.6 1.0
O5 A:HCA502 4.5 36.5 1.0
CE2 A:PHE381 4.5 21.7 1.0
S3A A:ICS501 4.5 29.0 1.0
ND1 A:HIS442 4.7 31.2 1.0
C3 A:HCA502 4.8 29.2 1.0
C7 A:HCA502 5.0 29.2 1.0

Iron binding site 7 out of 32 in 9cje

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Iron binding site 7 out of 32 in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:37.3
occ:1.00
FE7 A:ICS501 0.0 37.3 1.0
CX A:ICS501 2.0 30.4 1.0
S5A A:ICS501 2.2 26.6 1.0
S4B A:ICS501 2.2 23.3 1.0
S3B A:ICS501 2.3 17.7 1.0
FE3 A:ICS501 2.6 37.9 1.0
FE6 A:ICS501 2.6 42.5 1.0
FE5 A:ICS501 2.6 52.2 1.0
MO1 A:ICS501 2.7 56.8 1.0
O5 A:HCA502 3.7 36.5 1.0
FE2 A:ICS501 3.7 39.2 1.0
FE4 A:ICS501 3.7 39.8 1.0
O A:HOH687 3.8 14.1 1.0
S1B A:ICS501 3.8 33.8 1.0
NH2 A:ARG96 4.0 21.6 1.0
NE A:ARG96 4.0 23.9 1.0
S2A A:ICS501 4.3 24.2 1.0
S4A A:ICS501 4.3 18.9 1.0
S2B A:ICS501 4.4 22.7 1.0
O7 A:HCA502 4.5 30.6 1.0
CZ A:ARG96 4.5 13.2 1.0
S3A A:ICS501 4.5 29.0 1.0
CZ A:ARG359 4.6 26.9 1.0
ND1 A:HIS442 4.6 31.2 1.0
C7 A:HCA502 4.7 29.2 1.0
NH2 A:ARG359 4.7 20.3 1.0
NH1 A:ARG359 4.8 21.5 1.0
NE A:ARG359 4.8 30.2 1.0
FE1 A:ICS501 5.0 43.7 1.0

Iron binding site 8 out of 32 in 9cje

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Iron binding site 8 out of 32 in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe503

b:45.0
occ:1.00
FE1 A:CLF503 0.0 45.0 1.0
SG A:CYS154 2.3 24.9 1.0
S2A A:CLF503 2.3 14.4 1.0
S3A A:CLF503 2.3 20.7 1.0
S1 A:CLF503 2.4 29.9 1.0
FE2 A:CLF503 2.5 36.5 1.0
FE4 A:CLF503 2.6 31.9 1.0
FE3 A:CLF503 2.8 40.3 1.0
CB A:CYS154 3.1 19.1 1.0
O B:HOH718 3.5 25.7 1.0
N A:CYS154 3.7 23.9 1.0
CA A:GLY185 3.8 12.8 1.0
S4A A:CLF503 3.8 18.7 1.0
CA A:CYS154 3.9 16.7 1.0
OG B:SER92 3.9 35.5 1.0
N A:GLY185 4.0 16.1 1.0
SG B:CYS95 4.1 35.7 1.0
FE8 A:CLF503 4.4 37.2 1.0
SG A:CYS88 4.5 20.4 1.0
SG B:CYS153 4.6 31.0 1.0
FE5 A:CLF503 4.7 35.9 1.0
C A:GLY185 4.7 24.3 1.0
CB B:SER92 4.8 28.2 1.0
C A:GLU153 4.8 19.9 1.0
FE6 A:CLF503 4.9 55.5 1.0
N A:PHE186 4.9 27.7 1.0
SG A:CYS62 4.9 17.3 1.0

Iron binding site 9 out of 32 in 9cje

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Iron binding site 9 out of 32 in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe503

b:36.5
occ:1.00
FE2 A:CLF503 0.0 36.5 1.0
S4A A:CLF503 2.3 18.7 1.0
SG B:CYS95 2.3 35.7 1.0
S2A A:CLF503 2.3 14.4 1.0
S1 A:CLF503 2.5 29.9 1.0
FE1 A:CLF503 2.5 45.0 1.0
FE4 A:CLF503 2.6 31.9 1.0
FE3 A:CLF503 2.8 40.3 1.0
FE8 A:CLF503 3.0 37.2 1.0
N B:CYS95 3.2 19.9 1.0
CB B:CYS95 3.5 18.7 1.0
CA B:CYS95 3.5 24.4 1.0
S3A A:CLF503 3.8 20.7 1.0
FE5 A:CLF503 3.8 35.9 1.0
C B:GLY94 3.9 17.3 1.0
S4B A:CLF503 4.0 12.5 1.0
O B:HOH718 4.0 25.7 1.0
OG B:SER92 4.1 35.5 1.0
CA B:GLY94 4.4 14.0 1.0
SG A:CYS88 4.5 20.4 1.0
SG A:CYS154 4.5 24.9 1.0
FE6 A:CLF503 4.6 55.5 1.0
O B:GLY94 4.6 27.9 1.0
SG A:CYS62 4.7 17.3 1.0
N B:GLY94 4.9 22.3 1.0
CB B:SER92 5.0 28.2 1.0

Iron binding site 10 out of 32 in 9cje

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Iron binding site 10 out of 32 in the Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Cryoem Structure of Nitrogenase Mofe-Protein 20 Second Time Point Under Alkaline Turnover within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe503

b:40.3
occ:1.00
FE3 A:CLF503 0.0 40.3 1.0
S4A A:CLF503 2.3 18.7 1.0
SG A:CYS62 2.3 17.3 1.0
S2A A:CLF503 2.3 14.4 1.0
S3A A:CLF503 2.3 20.7 1.0
FE4 A:CLF503 2.7 31.9 1.0
FE2 A:CLF503 2.8 36.5 1.0
FE1 A:CLF503 2.8 45.0 1.0
CB A:CYS62 3.2 17.1 1.0
CA A:GLY185 3.7 12.8 1.0
CB A:TYR64 3.9 11.8 1.0
S1 A:CLF503 4.2 29.9 1.0
CD2 A:TYR64 4.3 12.1 1.0
N A:GLY185 4.3 16.1 1.0
CA B:GLY94 4.4 14.0 1.0
CG A:TYR64 4.5 15.6 1.0
CA A:CYS62 4.6 18.4 1.0
C B:GLY94 4.6 17.3 1.0
SG A:CYS154 4.7 24.9 1.0
N B:CYS95 4.7 19.9 1.0
N A:TYR64 4.7 23.4 1.0
C A:GLY185 4.8 24.3 1.0
SG A:CYS88 4.8 20.4 1.0
CA A:TYR64 4.9 12.8 1.0
O B:HOH836 4.9 10.2 1.0
SG B:CYS95 4.9 35.7 1.0

Reference:

R.A.Warmack, D.C.Rees. Structural Evolution of Nitrogenase States Under Alkaline Turnover. Nat Commun V. 15 10472 2024.
ISSN: ESSN 2041-1723
PubMed: 39622820
DOI: 10.1038/S41467-024-54713-0
Page generated: Sat Feb 8 18:53:41 2025

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