Iron in PDB 9cu0: Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)

All present enzymatic activity of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry):
1.18.6.1;

The structure of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Magnesium	(Mg)	2 atoms

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 Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) (pdb code 9cu0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 38 binding sites of Iron where determined in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry), PDB code: 9cu0:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 38 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:102.6 occ:1.00 FE1 A:ICS502 0.0 102.6 1.0 S2A A:ICS502 2.3 102.6 1.0 S4A A:ICS502 2.3 102.6 1.0 S1A A:ICS502 2.3 102.6 1.0 SG A:CYS275 2.3 96.6 1.0 FE4 A:ICS502 2.6 102.6 1.0 FE3 A:ICS502 2.6 102.6 1.0 FE2 A:ICS502 2.7 102.6 1.0 CX A:ICS502 3.4 102.6 1.0 CB A:CYS275 3.6 96.6 1.0 O A:GLY357 3.8 96.8 1.0 CB A:SER278 4.0 96.2 1.0 OG A:SER278 4.1 96.2 1.0 N A:SER278 4.6 96.2 1.0 C A:GLY357 4.7 96.8 1.0 S3A A:ICS502 4.8 102.6 1.0 CE2 A:TYR229 4.8 94.6 1.0 S5A A:ICS502 4.8 102.6 1.0 S2B A:ICS502 4.8 102.6 1.0 CA A:CYS275 4.9 96.6 1.0 CA A:SER278 4.9 96.2 1.0 FE7 A:ICS502 5.0 102.6 1.0 FE6 A:ICS502 5.0 102.6 1.0 FE5 A:ICS502 5.0 102.6 1.0

Iron binding site 2 out of 38 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:102.6 occ:1.00 FE2 A:ICS502 0.0 102.6 1.0 CX A:ICS502 2.0 102.6 1.0 S2B A:ICS502 2.2 102.6 1.0 S2A A:ICS502 2.2 102.6 1.0 S1A A:ICS502 2.3 102.6 1.0 FE6 A:ICS502 2.6 102.6 1.0 FE4 A:ICS502 2.6 102.6 1.0 FE1 A:ICS502 2.7 102.6 1.0 FE3 A:ICS502 2.7 102.6 1.0 FE5 A:ICS502 3.7 102.6 1.0 FE7 A:ICS502 3.7 102.6 1.0 CE1 A:HIS195 3.8 92.2 1.0 S4A A:ICS502 3.9 102.6 1.0 NE2 A:HIS195 4.0 92.2 1.0 S3B A:ICS502 4.2 102.6 1.0 S1B A:ICS502 4.2 102.6 1.0 CZ A:PHE381 4.3 95.9 1.0 CG1 A:VAL70 4.4 90.3 1.0 S3A A:ICS502 4.5 102.6 1.0 S5A A:ICS502 4.5 102.6 1.0 CE1 A:PHE381 4.6 95.9 1.0 SG A:CYS275 4.8 96.6 1.0 ND1 A:HIS195 4.9 92.2 1.0 MO1 A:ICS502 5.0 102.6 1.0 O A:GLY357 5.0 96.8 1.0 CB A:SER278 5.0 96.2 1.0

Iron binding site 3 out of 38 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:102.6 occ:1.00 FE3 A:ICS502 0.0 102.6 1.0 CX A:ICS502 2.0 102.6 1.0 S5A A:ICS502 2.2 102.6 1.0 S4A A:ICS502 2.2 102.6 1.0 S2A A:ICS502 2.3 102.6 1.0 FE7 A:ICS502 2.6 102.6 1.0 FE4 A:ICS502 2.6 102.6 1.0 FE1 A:ICS502 2.6 102.6 1.0 FE2 A:ICS502 2.7 102.6 1.0 FE6 A:ICS502 3.7 102.6 1.0 FE5 A:ICS502 3.7 102.6 1.0 S1A A:ICS502 3.8 102.6 1.0 S3B A:ICS502 4.2 102.6 1.0 S4B A:ICS502 4.2 102.6 1.0 CE2 A:TYR229 4.3 94.6 1.0 CD2 A:TYR229 4.3 94.6 1.0 NH2 A:ARG359 4.4 93.2 1.0 S2B A:ICS502 4.4 102.6 1.0 S3A A:ICS502 4.5 102.6 1.0 SG A:CYS275 4.5 96.6 1.0 MO1 A:ICS502 5.0 102.6 1.0

Iron binding site 4 out of 38 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:102.6 occ:1.00 FE4 A:ICS502 0.0 102.6 1.0 CX A:ICS502 2.0 102.6 1.0 S3A A:ICS502 2.2 102.6 1.0 S4A A:ICS502 2.3 102.6 1.0 S1A A:ICS502 2.3 102.6 1.0 FE5 A:ICS502 2.6 102.6 1.0 FE1 A:ICS502 2.6 102.6 1.0 FE3 A:ICS502 2.6 102.6 1.0 FE2 A:ICS502 2.6 102.6 1.0 O A:GLY357 2.9 96.8 1.0 N A:GLY357 3.6 96.8 1.0 FE7 A:ICS502 3.7 102.6 1.0 FE6 A:ICS502 3.7 102.6 1.0 S2A A:ICS502 3.8 102.6 1.0 C A:GLY357 3.8 96.8 1.0 CA A:GLY357 4.1 96.8 1.0 S4B A:ICS502 4.2 102.6 1.0 S1B A:ICS502 4.3 102.6 1.0 S5A A:ICS502 4.5 102.6 1.0 S2B A:ICS502 4.5 102.6 1.0 SG A:CYS275 4.6 96.6 1.0 C A:GLY356 4.7 97.1 1.0 CB A:ARG359 4.9 93.2 1.0 CA A:GLY356 4.9 97.1 1.0 N A:ARG359 4.9 93.2 1.0 CZ A:PHE381 5.0 95.9 1.0

Iron binding site 5 out of 38 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:102.6 occ:1.00 FE5 A:ICS502 0.0 102.6 1.0 CX A:ICS502 2.0 102.6 1.0 S4B A:ICS502 2.2 102.6 1.0 S3A A:ICS502 2.3 102.6 1.0 S1B A:ICS502 2.3 102.6 1.0 FE4 A:ICS502 2.6 102.6 1.0 FE6 A:ICS502 2.6 102.6 1.0 FE7 A:ICS502 2.6 102.6 1.0 MO1 A:ICS502 2.7 102.6 1.0 FE2 A:ICS502 3.7 102.6 1.0 FE3 A:ICS502 3.7 102.6 1.0 S3B A:ICS502 3.8 102.6 1.0 ND1 A:HIS442 4.1 95.7 1.0 CG2 A:ILE355 4.2 94.5 1.0 N A:GLY356 4.2 97.1 1.0 S1A A:ICS502 4.3 102.6 1.0 CA A:GLY356 4.3 97.1 1.0 S4A A:ICS502 4.3 102.6 1.0 N A:GLY357 4.4 96.8 1.0 S2B A:ICS502 4.4 102.6 1.0 S5A A:ICS502 4.5 102.6 1.0 CE1 A:HIS442 4.5 95.7 1.0 CZ A:ARG359 4.7 93.2 1.0 NH1 A:ARG359 4.8 93.2 1.0 NE A:ARG359 4.8 93.2 1.0 C A:GLY356 4.9 97.1 1.0 O A:GLY357 4.9 96.8 1.0 FE1 A:ICS502 5.0 102.6 1.0 CG A:HIS442 5.0 95.7 1.0 O7 A:HCA501 5.0 99.6 1.0

Iron binding site 6 out of 38 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:102.6 occ:1.00 FE6 A:ICS502 0.0 102.6 1.0 CX A:ICS502 2.0 102.6 1.0 S2B A:ICS502 2.2 102.6 1.0 S3B A:ICS502 2.2 102.6 1.0 S1B A:ICS502 2.2 102.6 1.0 FE2 A:ICS502 2.6 102.6 1.0 FE7 A:ICS502 2.6 102.6 1.0 FE5 A:ICS502 2.6 102.6 1.0 MO1 A:ICS502 2.6 102.6 1.0 O1 A:HCA501 3.4 99.6 1.0 FE3 A:ICS502 3.7 102.6 1.0 FE4 A:ICS502 3.7 102.6 1.0 S4B A:ICS502 3.8 102.6 1.0 S2A A:ICS502 4.2 102.6 1.0 S1A A:ICS502 4.3 102.6 1.0 O7 A:HCA501 4.3 99.6 1.0 C1 A:HCA501 4.4 99.6 1.0 CG2 A:VAL70 4.4 90.3 1.0 S5A A:ICS502 4.5 102.6 1.0 S3A A:ICS502 4.5 102.6 1.0 C2 A:HCA501 4.5 99.6 1.0 CZ A:PHE381 4.6 95.9 1.0 NE2 A:GLN191 4.9 91.2 1.0 FE1 A:ICS502 5.0 102.6 1.0 C3 A:HCA501 5.0 99.6 1.0

Iron binding site 7 out of 38 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:102.6 occ:1.00 FE7 A:ICS502 0.0 102.6 1.0 CX A:ICS502 2.0 102.6 1.0 S5A A:ICS502 2.2 102.6 1.0 S4B A:ICS502 2.2 102.6 1.0 S3B A:ICS502 2.2 102.6 1.0 FE3 A:ICS502 2.6 102.6 1.0 FE6 A:ICS502 2.6 102.6 1.0 FE5 A:ICS502 2.6 102.6 1.0 MO1 A:ICS502 2.6 102.6 1.0 FE2 A:ICS502 3.7 102.6 1.0 FE4 A:ICS502 3.7 102.6 1.0 S1B A:ICS502 3.8 102.6 1.0 S2A A:ICS502 4.3 102.6 1.0 S4A A:ICS502 4.3 102.6 1.0 S2B A:ICS502 4.4 102.6 1.0 NH2 A:ARG359 4.4 93.2 1.0 NE A:ARG96 4.4 91.7 1.0 NH1 A:ARG359 4.5 93.2 1.0 S3A A:ICS502 4.5 102.6 1.0 CZ A:ARG359 4.6 93.2 1.0 O5 A:HCA501 4.8 99.6 1.0 FE1 A:ICS502 5.0 102.6 1.0 CD A:ARG96 5.0 91.7 1.0

Iron binding site 8 out of 38 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe503 b:89.6 occ:1.00 FE1 A:CLF503 0.0 89.6 1.0 S3A A:CLF503 2.3 89.6 1.0 S2A A:CLF503 2.3 89.6 1.0 FE4 A:CLF503 2.4 89.6 1.0 S1 A:CLF503 2.5 89.6 1.0 FE2 A:CLF503 2.5 89.6 1.0 FE3 A:CLF503 2.7 89.6 1.0 SG B:CYS95 3.0 86.0 1.0 FE8 A:CLF503 3.2 89.6 1.0 N B:CYS95 3.2 86.0 1.0 CA B:CYS95 3.7 86.0 1.0 C B:GLY94 3.7 86.3 1.0 S4A A:CLF503 3.7 89.6 1.0 CB B:CYS95 3.9 86.0 1.0 CA B:GLY94 4.1 86.3 1.0 S4B A:CLF503 4.2 89.6 1.0 SG A:CYS62 4.3 93.1 1.0 FE5 A:CLF503 4.3 89.6 1.0 O B:GLY94 4.4 86.3 1.0 CB A:CYS62 4.7 93.1 1.0 N B:GLY94 4.7 86.3 1.0 SG A:CYS154 4.8 87.8 1.0 SG A:CYS88 5.0 84.7 1.0

Iron binding site 9 out of 38 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe503 b:89.6 occ:1.00 FE2 A:CLF503 0.0 89.6 1.0 S2A A:CLF503 2.3 89.6 1.0 S4A A:CLF503 2.3 89.6 1.0 SG A:CYS154 2.3 87.8 1.0 S1 A:CLF503 2.4 89.6 1.0 FE1 A:CLF503 2.5 89.6 1.0 FE4 A:CLF503 2.6 89.6 1.0 FE3 A:CLF503 2.8 89.6 1.0 CB A:CYS154 3.7 87.8 1.0 S3A A:CLF503 3.8 89.6 1.0 CA A:GLY185 3.9 97.6 1.0 N A:GLY185 4.1 97.6 1.0 SG B:CYS95 4.2 86.0 1.0 FE8 A:CLF503 4.4 89.6 1.0 N A:CYS154 4.4 87.8 1.0 OG B:SER92 4.7 87.1 1.0 CB B:SER92 4.7 87.1 1.0 SG B:CYS153 4.7 90.3 1.0 CA A:CYS154 4.7 87.8 1.0 C A:GLY185 4.8 97.6 1.0

Iron binding site 10 out of 38 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe503 b:89.6 occ:1.00 FE3 A:CLF503 0.0 89.6 1.0 S3A A:CLF503 2.2 89.6 1.0 S2A A:CLF503 2.3 89.6 1.0 S4A A:CLF503 2.3 89.6 1.0 SG A:CYS62 2.3 93.1 1.0 FE4 A:CLF503 2.7 89.6 1.0 FE1 A:CLF503 2.7 89.6 1.0 FE2 A:CLF503 2.8 89.6 1.0 CB A:CYS62 3.0 93.1 1.0 CA A:GLY185 3.5 97.6 1.0 CB A:TYR64 3.8 82.7 1.0 N A:GLY185 4.1 97.6 1.0 S1 A:CLF503 4.2 89.6 1.0 CA A:CYS62 4.4 93.1 1.0 SG A:CYS154 4.5 87.8 1.0 CG A:TYR64 4.6 82.7 1.0 N A:TYR64 4.6 82.7 1.0 CD2 A:TYR64 4.6 82.7 1.0 CA B:GLY94 4.6 86.3 1.0 C A:GLY185 4.7 97.6 1.0 CA A:TYR64 4.8 82.7 1.0 C A:CYS62 4.9 93.1 1.0 C B:GLY94 5.0 86.3 1.0

S.M.Narehood, B.D.Cook, S.Srisantitham, V.H.Eng, A.Shiau, K.L.Mcguire, R.D.Britt, M.A.Herzik, F.A.Tezcan. Structural Basis For the Conformational Protection of Nitrogenase From O2 Nature 2025.
ISSN: ESSN 1476-4687
DOI: 10.1038/S41586-024-08311-1