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Iron in PDB 8enm: Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions

Enzymatic activity of Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions

All present enzymatic activity of Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions:
1.18.6.1;

Other elements in 8enm:

The structure of Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions 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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions (pdb code 8enm). 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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions, PDB code: 8enm:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 32 in 8enm

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Iron binding site 1 out of 32 in the Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions


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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:73.6
occ:1.00
FE1 A:ICS600 0.0 73.6 1.0
SG A:CYS275 2.1 58.4 1.0
S2A A:ICS600 2.3 52.1 1.0
S4A A:ICS600 2.3 49.1 1.0
S1A A:ICS600 2.3 52.4 1.0
FE4 A:ICS600 2.7 71.0 1.0
FE3 A:ICS600 2.7 68.8 1.0
FE2 A:ICS600 2.7 67.9 1.0
CB A:CYS275 3.2 45.4 1.0
CX A:ICS600 3.4 57.8 1.0
CB A:LEU358 4.0 50.0 1.0
OG A:SER278 4.1 57.9 1.0
CB A:SER278 4.3 46.1 1.0
CA A:CYS275 4.5 47.8 1.0
CE2 A:TYR229 4.5 35.4 1.0
CD2 A:LEU358 4.7 48.0 1.0
N A:LEU358 4.8 51.5 1.0
S3A A:ICS600 4.8 58.3 1.0
S2B A:ICS600 4.8 48.2 1.0
S5A A:ICS600 4.8 54.6 1.0
N A:SER278 4.9 49.3 1.0
CG A:LEU358 5.0 56.0 1.0
FE6 A:ICS600 5.0 67.3 1.0
FE7 A:ICS600 5.0 67.7 1.0

Iron binding site 2 out of 32 in 8enm

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Iron binding site 2 out of 32 in the Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions


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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:67.9
occ:1.00
FE2 A:ICS600 0.0 67.9 1.0
CX A:ICS600 2.0 57.8 1.0
S2B A:ICS600 2.2 48.2 1.0
S2A A:ICS600 2.2 52.1 1.0
S1A A:ICS600 2.3 52.4 1.0
FE6 A:ICS600 2.6 67.3 1.0
FE4 A:ICS600 2.7 71.0 1.0
FE1 A:ICS600 2.7 73.6 1.0
FE3 A:ICS600 2.7 68.8 1.0
FE5 A:ICS600 3.7 69.2 1.0
FE7 A:ICS600 3.7 67.7 1.0
S4A A:ICS600 3.9 49.1 1.0
CE1 A:HIS195 3.9 41.4 1.0
CZ A:PHE381 4.0 53.1 1.0
NE2 A:HIS195 4.0 52.3 1.0
S1B A:ICS600 4.2 48.9 1.0
S3B A:ICS600 4.2 46.5 1.0
CE1 A:PHE381 4.4 54.0 1.0
SG A:CYS275 4.5 58.4 1.0
CG1 A:VAL70 4.5 42.7 1.0
S3A A:ICS600 4.5 58.3 1.0
S5A A:ICS600 4.5 54.6 1.0
CG2 A:VAL70 4.8 35.8 1.0
N A:GLY357 5.0 52.6 1.0

Iron binding site 3 out of 32 in 8enm

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Iron binding site 3 out of 32 in the Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions


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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:68.8
occ:1.00
FE3 A:ICS600 0.0 68.8 1.0
CX A:ICS600 2.0 57.8 1.0
S5A A:ICS600 2.2 54.6 1.0
S4A A:ICS600 2.3 49.1 1.0
S2A A:ICS600 2.3 52.1 1.0
FE7 A:ICS600 2.6 67.7 1.0
FE4 A:ICS600 2.6 71.0 1.0
FE1 A:ICS600 2.7 73.6 1.0
FE2 A:ICS600 2.7 67.9 1.0
FE6 A:ICS600 3.7 67.3 1.0
FE5 A:ICS600 3.7 69.2 1.0
NH2 A:ARG96 3.8 47.6 1.0
S1A A:ICS600 3.9 52.4 1.0
O A:HOH952 4.0 51.7 1.0
CD2 A:TYR229 4.2 41.6 1.0
S4B A:ICS600 4.2 46.9 1.0
S3B A:ICS600 4.2 46.5 1.0
CE2 A:TYR229 4.4 35.4 1.0
S2B A:ICS600 4.5 48.2 1.0
S3A A:ICS600 4.5 58.3 1.0
SG A:CYS275 4.6 58.4 1.0
NE A:ARG359 4.9 54.9 1.0
CZ A:ARG96 5.0 47.4 1.0
NH2 A:ARG359 5.0 54.4 1.0

Iron binding site 4 out of 32 in 8enm

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Iron binding site 4 out of 32 in the Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions


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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:71.0
occ:1.00
FE4 A:ICS600 0.0 71.0 1.0
CX A:ICS600 2.0 57.8 1.0
S3A A:ICS600 2.2 58.3 1.0
S4A A:ICS600 2.3 49.1 1.0
S1A A:ICS600 2.3 52.4 1.0
FE5 A:ICS600 2.6 69.2 1.0
FE3 A:ICS600 2.6 68.8 1.0
FE1 A:ICS600 2.7 73.6 1.0
FE2 A:ICS600 2.7 67.9 1.0
FE7 A:ICS600 3.7 67.7 1.0
FE6 A:ICS600 3.7 67.3 1.0
N A:LEU358 3.8 51.5 1.0
S2A A:ICS600 3.8 52.1 1.0
N A:GLY357 3.9 52.6 1.0
CB A:LEU358 4.0 50.0 1.0
S4B A:ICS600 4.2 46.9 1.0
S1B A:ICS600 4.3 48.9 1.0
CA A:LEU358 4.5 49.6 1.0
S5A A:ICS600 4.5 54.6 1.0
SG A:CYS275 4.5 58.4 1.0
S2B A:ICS600 4.5 48.2 1.0
C A:GLY357 4.6 51.0 1.0
CA A:GLY357 4.6 47.4 1.0
N A:ARG359 4.6 53.9 1.0
CG A:ARG359 4.8 52.3 1.0
NE A:ARG359 4.9 54.9 1.0
CD A:ARG359 4.9 46.8 1.0
C A:GLY356 4.9 49.5 1.0
CZ A:PHE381 5.0 53.1 1.0
CA A:GLY356 5.0 48.5 1.0

Iron binding site 5 out of 32 in 8enm

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Iron binding site 5 out of 32 in the Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions


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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:69.2
occ:1.00
FE5 A:ICS600 0.0 69.2 1.0
CX A:ICS600 2.0 57.8 1.0
S4B A:ICS600 2.3 46.9 1.0
S3A A:ICS600 2.3 58.3 1.0
S1B A:ICS600 2.3 48.9 1.0
FE4 A:ICS600 2.6 71.0 1.0
FE7 A:ICS600 2.6 67.7 1.0
FE6 A:ICS600 2.6 67.3 1.0
MO1 A:ICS600 2.7 71.1 1.0
FE2 A:ICS600 3.7 67.9 1.0
FE3 A:ICS600 3.7 68.8 1.0
ND1 A:HIS442 3.8 49.2 1.0
S3B A:ICS600 3.9 46.5 1.0
N A:GLY356 4.0 51.5 1.0
CE1 A:HIS442 4.0 46.0 1.0
CA A:GLY356 4.2 48.5 1.0
CG2 A:ILE355 4.2 46.6 1.0
S1A A:ICS600 4.3 52.4 1.0
S4A A:ICS600 4.3 49.1 1.0
S2B A:ICS600 4.5 48.2 1.0
S5A A:ICS600 4.5 54.6 1.0
N A:GLY357 4.6 52.6 1.0
CD A:ARG359 4.6 46.8 1.0
O7 A:HCA601 4.6 58.8 1.0
CG A:HIS442 4.7 43.4 1.0
O6 A:HCA601 4.8 53.3 1.0
NE A:ARG359 4.8 54.9 1.0
C A:GLY356 4.9 49.5 1.0
CZ A:PHE381 5.0 53.1 1.0

Iron binding site 6 out of 32 in 8enm

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Iron binding site 6 out of 32 in the Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions


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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:67.3
occ:1.00
FE6 A:ICS600 0.0 67.3 1.0
CX A:ICS600 2.0 57.8 1.0
S2B A:ICS600 2.2 48.2 1.0
S3B A:ICS600 2.2 46.5 1.0
S1B A:ICS600 2.2 48.9 1.0
FE2 A:ICS600 2.6 67.9 1.0
FE7 A:ICS600 2.6 67.7 1.0
FE5 A:ICS600 2.6 69.2 1.0
MO1 A:ICS600 2.7 71.1 1.0
FE3 A:ICS600 3.7 68.8 1.0
O7 A:HCA601 3.7 58.8 1.0
FE4 A:ICS600 3.7 71.0 1.0
S4B A:ICS600 3.8 46.9 1.0
O2 A:HCA601 4.1 65.3 1.0
CZ A:PHE381 4.1 53.1 1.0
S2A A:ICS600 4.2 52.1 1.0
S1A A:ICS600 4.3 52.4 1.0
CG2 A:VAL70 4.4 35.8 1.0
O6 A:HCA601 4.4 53.3 1.0
S5A A:ICS600 4.4 54.6 1.0
S3A A:ICS600 4.5 58.3 1.0
CE2 A:PHE381 4.6 49.7 1.0
ND1 A:HIS442 4.7 49.2 1.0
C3 A:HCA601 4.8 56.5 1.0
C1 A:HCA601 4.9 58.9 1.0
C7 A:HCA601 5.0 53.2 1.0
FE1 A:ICS600 5.0 73.6 1.0

Iron binding site 7 out of 32 in 8enm

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Iron binding site 7 out of 32 in the Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions


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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:67.7
occ:1.00
FE7 A:ICS600 0.0 67.7 1.0
CX A:ICS600 2.0 57.8 1.0
S5A A:ICS600 2.2 54.6 1.0
S4B A:ICS600 2.2 46.9 1.0
S3B A:ICS600 2.3 46.5 1.0
FE3 A:ICS600 2.6 68.8 1.0
FE6 A:ICS600 2.6 67.3 1.0
FE5 A:ICS600 2.6 69.2 1.0
MO1 A:ICS600 2.7 71.1 1.0
FE2 A:ICS600 3.7 67.9 1.0
FE4 A:ICS600 3.7 71.0 1.0
O6 A:HCA601 3.7 53.3 1.0
O A:HOH763 3.7 43.4 1.0
S1B A:ICS600 3.8 48.9 1.0
NH2 A:ARG96 3.9 47.6 1.0
NE A:ARG96 4.0 50.1 1.0
S2A A:ICS600 4.3 52.1 1.0
S4A A:ICS600 4.3 49.1 1.0
S2B A:ICS600 4.4 48.2 1.0
CZ A:ARG96 4.5 47.4 1.0
S3A A:ICS600 4.5 58.3 1.0
O7 A:HCA601 4.6 58.8 1.0
CZ A:ARG359 4.6 50.0 1.0
NH2 A:ARG359 4.6 54.4 1.0
C7 A:HCA601 4.7 53.2 1.0
ND1 A:HIS442 4.7 49.2 1.0
NE A:ARG359 4.8 54.9 1.0
NH1 A:ARG359 4.9 51.7 1.0
FE1 A:ICS600 5.0 73.6 1.0

Iron binding site 8 out of 32 in 8enm

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Iron binding site 8 out of 32 in the Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions


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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe600

b:61.0
occ:1.00
FE1 B:CLF600 0.0 61.0 1.0
SG A:CYS154 2.3 48.0 1.0
S2A B:CLF600 2.3 38.9 1.0
S3A B:CLF600 2.3 44.4 1.0
S1 B:CLF600 2.4 46.9 1.0
FE2 B:CLF600 2.5 64.2 1.0
FE4 B:CLF600 2.6 66.4 1.0
FE3 B:CLF600 2.8 59.9 1.0
CB A:CYS154 3.3 31.1 1.0
O B:HOH933 3.6 28.1 1.0
CA A:GLY185 3.8 42.9 1.0
N A:CYS154 3.8 44.0 1.0
S4A B:CLF600 3.8 35.9 1.0
OG B:SER92 3.9 47.5 1.0
N A:GLY185 4.0 44.2 1.0
SG B:CYS95 4.0 42.9 1.0
CA A:CYS154 4.1 39.0 1.0
FE8 B:CLF600 4.4 63.2 1.0
SG A:CYS88 4.4 52.2 1.0
FE5 B:CLF600 4.7 66.6 1.0
C A:GLY185 4.7 45.8 1.0
SG B:CYS153 4.7 42.1 1.0
CB B:SER92 4.8 36.5 1.0
FE6 B:CLF600 4.9 71.7 1.0
C A:GLU153 4.9 40.0 1.0
N A:PHE186 4.9 46.5 1.0
SG A:CYS62 4.9 42.5 1.0

Iron binding site 9 out of 32 in 8enm

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Iron binding site 9 out of 32 in the Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions


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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe600

b:64.2
occ:1.00
FE2 B:CLF600 0.0 64.2 1.0
SG B:CYS95 2.2 42.9 1.0
S4A B:CLF600 2.3 35.9 1.0
S2A B:CLF600 2.3 38.9 1.0
S1 B:CLF600 2.5 46.9 1.0
FE1 B:CLF600 2.5 61.0 1.0
FE4 B:CLF600 2.6 66.4 1.0
FE3 B:CLF600 2.7 59.9 1.0
FE8 B:CLF600 2.9 63.2 1.0
N B:CYS95 3.2 33.5 1.0
CB B:CYS95 3.4 30.2 1.0
CA B:CYS95 3.5 24.6 1.0
S3A B:CLF600 3.8 44.4 1.0
FE5 B:CLF600 3.8 66.6 1.0
C B:GLY94 3.9 23.7 1.0
S4B B:CLF600 4.0 39.1 1.0
OG B:SER92 4.1 47.5 1.0
O B:HOH933 4.2 28.1 1.0
SG A:CYS88 4.4 52.2 1.0
CA B:GLY94 4.4 19.1 1.0
SG A:CYS154 4.5 48.0 1.0
FE6 B:CLF600 4.6 71.7 1.0
O B:GLY94 4.6 36.1 1.0
SG A:CYS62 4.8 42.5 1.0
N B:GLY94 4.8 26.3 1.0
CB B:SER92 5.0 36.5 1.0
O B:SER92 5.0 44.0 1.0

Iron binding site 10 out of 32 in 8enm

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Iron binding site 10 out of 32 in the Cryoem Structure of the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions


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 the High pH Nitrogenase Mofe-Protein Under Non- Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe600

b:59.9
occ:1.00
FE3 B:CLF600 0.0 59.9 1.0
S4A B:CLF600 2.3 35.9 1.0
SG A:CYS62 2.3 42.5 1.0
S2A B:CLF600 2.3 38.9 1.0
S3A B:CLF600 2.3 44.4 1.0
FE4 B:CLF600 2.7 66.4 1.0
FE2 B:CLF600 2.7 64.2 1.0
FE1 B:CLF600 2.8 61.0 1.0
CB A:CYS62 3.2 32.5 1.0
CA A:GLY185 3.8 42.9 1.0
CB A:TYR64 4.0 37.6 1.0
S1 B:CLF600 4.2 46.9 1.0
CA B:GLY94 4.3 19.1 1.0
N A:GLY185 4.5 44.2 1.0
CD1 A:TYR64 4.5 35.1 1.0
C B:GLY94 4.5 23.7 1.0
CG A:TYR64 4.6 36.9 1.0
N B:CYS95 4.6 33.5 1.0
CA A:CYS62 4.7 31.7 1.0
SG A:CYS154 4.7 48.0 1.0
O B:HOH1004 4.8 38.3 1.0
SG A:CYS88 4.8 52.2 1.0
N A:TYR64 4.8 36.3 1.0
C A:GLY185 4.9 45.8 1.0
SG B:CYS95 4.9 42.9 1.0
CE2 B:TYR98 5.0 24.3 1.0
CA A:TYR64 5.0 27.4 1.0

Reference:

R.A.Warmack, A.O.Maggiolo, A.Orta, B.B.Wenke, J.B.Howard, D.C.Rees. Structural Consequences of Turnover-Induced Homocitrate Loss in Nitrogenase. Nat Commun V. 14 1091 2023.
ISSN: ESSN 2041-1723
PubMed: 36841829
DOI: 10.1038/S41467-023-36636-4
Page generated: Sat Aug 10 01:51:19 2024

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