Iron in PDB 11ne: Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact

All present enzymatic activity of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact:
1.18.6.1;

The structure of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact also contains other interesting chemical elements:

Molybdenum

(Mo)

2 atoms

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 Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact (pdb code 11ne). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 32 binding sites of Iron where determined in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact, PDB code: 11ne:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 32 in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:78.0 occ:1.00 FE1 A:ICS502 0.0 78.0 1.0 S2A A:ICS502 2.3 52.9 1.0 SG A:CYS275 2.3 48.7 1.0 S4A A:ICS502 2.3 59.6 1.0 S1A A:ICS502 2.3 51.3 1.0 FE4 A:ICS502 2.6 79.9 1.0 FE2 A:ICS502 2.7 66.9 1.0 FE3 A:ICS502 2.7 83.2 1.0 CB A:CYS275 3.4 34.9 1.0 CX A:ICS502 3.5 66.5 1.0 CB A:LEU358 4.3 57.5 1.0 CB A:SER278 4.3 32.1 1.0 OG A:SER278 4.5 39.2 1.0 N A:LEU358 4.5 64.7 1.0 CE2 A:TYR229 4.6 26.4 1.0 CA A:CYS275 4.7 33.1 1.0 S3A A:ICS502 4.8 64.1 1.0 S2B A:ICS502 4.8 51.0 1.0 S5A A:ICS502 4.8 57.2 1.0 FE6 A:ICS502 5.0 75.6 1.0 N A:SER278 5.0 31.5 1.0

Iron binding site 2 out of 32 in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:66.9 occ:1.00 FE2 A:ICS502 0.0 66.9 1.0 CX A:ICS502 2.0 66.5 1.0 S2B A:ICS502 2.2 51.0 1.0 S2A A:ICS502 2.2 52.9 1.0 S1A A:ICS502 2.3 51.3 1.0 FE6 A:ICS502 2.6 75.6 1.0 FE4 A:ICS502 2.7 79.9 1.0 FE1 A:ICS502 2.7 78.0 1.0 FE3 A:ICS502 2.7 83.2 1.0 FE5 A:ICS502 3.7 77.4 1.0 FE7 A:ICS502 3.7 73.7 1.0 S4A A:ICS502 3.9 59.6 1.0 CE1 A:HIS195 3.9 27.1 1.0 CZ A:PHE381 4.0 53.0 1.0 S1B A:ICS502 4.2 62.3 1.0 S3B A:ICS502 4.2 50.2 1.0 NE2 A:HIS195 4.2 27.2 1.0 CE1 A:PHE381 4.3 56.6 1.0 S3A A:ICS502 4.5 64.1 1.0 S5A A:ICS502 4.6 57.2 1.0 CG1 A:VAL70 4.7 21.7 1.0 SG A:CYS275 4.8 48.7 1.0 CG2 A:VAL70 4.8 22.6 1.0 ND1 A:HIS195 5.0 32.9 1.0

Iron binding site 3 out of 32 in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:83.2 occ:1.00 FE3 A:ICS502 0.0 83.2 1.0 CX A:ICS502 2.0 66.5 1.0 S5A A:ICS502 2.2 57.2 1.0 S4A A:ICS502 2.2 59.6 1.0 S2A A:ICS502 2.3 52.9 1.0 FE7 A:ICS502 2.6 73.7 1.0 FE4 A:ICS502 2.6 79.9 1.0 FE1 A:ICS502 2.7 78.0 1.0 FE2 A:ICS502 2.7 66.9 1.0 NH1 A:ARG359 3.6 44.9 1.0 FE6 A:ICS502 3.7 75.6 1.0 FE5 A:ICS502 3.7 77.4 1.0 S1A A:ICS502 3.9 51.3 1.0 NH2 A:ARG96 3.9 34.6 1.0 CD2 A:TYR229 4.1 24.4 1.0 CE2 A:TYR229 4.2 26.4 1.0 S3B A:ICS502 4.2 50.2 1.0 O A:HOH798 4.2 31.3 1.0 S4B A:ICS502 4.2 55.3 1.0 S3A A:ICS502 4.4 64.1 1.0 S2B A:ICS502 4.4 51.0 1.0 SG A:CYS275 4.7 48.7 1.0 CZ A:ARG359 4.8 46.2 1.0

Iron binding site 4 out of 32 in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:79.9 occ:1.00 FE4 A:ICS502 0.0 79.9 1.0 CX A:ICS502 2.0 66.5 1.0 S3A A:ICS502 2.2 64.1 1.0 S4A A:ICS502 2.3 59.6 1.0 S1A A:ICS502 2.3 51.3 1.0 FE5 A:ICS502 2.6 77.4 1.0 FE3 A:ICS502 2.6 83.2 1.0 FE1 A:ICS502 2.6 78.0 1.0 FE2 A:ICS502 2.7 66.9 1.0 FE7 A:ICS502 3.7 73.7 1.0 NH1 A:ARG359 3.7 44.9 1.0 FE6 A:ICS502 3.7 75.6 1.0 S2A A:ICS502 3.8 52.9 1.0 N A:LEU358 3.9 64.7 1.0 S4B A:ICS502 4.3 55.3 1.0 S1B A:ICS502 4.3 62.3 1.0 O A:GLY356 4.3 72.0 1.0 S5A A:ICS502 4.4 57.2 1.0 CB A:LEU358 4.5 57.5 1.0 S2B A:ICS502 4.5 51.0 1.0 CA A:GLY357 4.6 62.2 1.0 N A:ARG359 4.6 66.0 1.0 SG A:CYS275 4.6 48.7 1.0 C A:GLY357 4.7 63.4 1.0 CA A:LEU358 4.8 62.4 1.0 CZ A:ARG359 4.9 46.2 1.0 CD A:ARG359 5.0 55.5 1.0

Iron binding site 5 out of 32 in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:77.4 occ:1.00 FE5 A:ICS502 0.0 77.4 1.0 CX A:ICS502 2.0 66.5 1.0 S4B A:ICS502 2.2 55.3 1.0 S3A A:ICS502 2.2 64.1 1.0 S1B A:ICS502 2.3 62.3 1.0 FE6 A:ICS502 2.6 75.6 1.0 FE7 A:ICS502 2.6 73.7 1.0 FE4 A:ICS502 2.6 79.9 1.0 MO1 A:ICS502 2.7 88.4 1.0 FE2 A:ICS502 3.7 66.9 1.0 FE3 A:ICS502 3.7 83.2 1.0 ND1 A:HIS442 3.7 50.3 1.0 NH1 A:ARG359 3.8 44.9 1.0 S3B A:ICS502 3.8 50.2 1.0 CE1 A:HIS442 4.0 55.5 1.0 S1A A:ICS502 4.3 51.3 1.0 S4A A:ICS502 4.4 59.6 1.0 S5A A:ICS502 4.4 57.2 1.0 CD A:ARG359 4.4 55.5 1.0 S2B A:ICS502 4.4 51.0 1.0 CZ A:ARG359 4.5 46.2 1.0 CG2 A:ILE355 4.6 61.2 1.0 O A:ILE355 4.7 71.0 1.0 O A:GLY356 4.8 72.0 1.0 CG A:HIS442 4.8 48.7 1.0 NE A:ARG359 4.8 51.1 1.0 O7 A:HCA501 4.8 52.8 1.0

Iron binding site 6 out of 32 in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:75.6 occ:1.00 FE6 A:ICS502 0.0 75.6 1.0 CX A:ICS502 2.0 66.5 1.0 S2B A:ICS502 2.2 51.0 1.0 S3B A:ICS502 2.2 50.2 1.0 S1B A:ICS502 2.2 62.3 1.0 FE2 A:ICS502 2.6 66.9 1.0 FE7 A:ICS502 2.6 73.7 1.0 FE5 A:ICS502 2.6 77.4 1.0 MO1 A:ICS502 2.7 88.4 1.0 FE3 A:ICS502 3.7 83.2 1.0 O1 A:HCA501 3.7 57.9 1.0 FE4 A:ICS502 3.7 79.9 1.0 S4B A:ICS502 3.8 55.3 1.0 O7 A:HCA501 4.1 52.8 1.0 S2A A:ICS502 4.2 52.9 1.0 CZ A:PHE381 4.2 53.0 1.0 S1A A:ICS502 4.3 51.3 1.0 CG2 A:VAL70 4.4 22.6 1.0 S5A A:ICS502 4.5 57.2 1.0 S3A A:ICS502 4.5 64.1 1.0 CE2 A:PHE381 4.8 57.8 1.0 C1 A:HCA501 4.8 53.3 1.0 FE1 A:ICS502 5.0 78.0 1.0

Iron binding site 7 out of 32 in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:73.7 occ:1.00 FE7 A:ICS502 0.0 73.7 1.0 CX A:ICS502 2.0 66.5 1.0 S5A A:ICS502 2.2 57.2 1.0 S4B A:ICS502 2.2 55.3 1.0 S3B A:ICS502 2.3 50.2 1.0 FE3 A:ICS502 2.6 83.2 1.0 FE6 A:ICS502 2.6 75.6 1.0 FE5 A:ICS502 2.6 77.4 1.0 MO1 A:ICS502 2.7 88.4 1.0 O A:HOH661 3.5 34.5 1.0 NH1 A:ARG359 3.6 44.9 1.0 FE4 A:ICS502 3.7 79.9 1.0 FE2 A:ICS502 3.7 66.9 1.0 S1B A:ICS502 3.8 62.3 1.0 NH2 A:ARG96 3.9 34.6 1.0 NE A:ARG96 3.9 36.1 1.0 S2A A:ICS502 4.3 52.9 1.0 S4A A:ICS502 4.3 59.6 1.0 CZ A:ARG359 4.4 46.2 1.0 S2B A:ICS502 4.4 51.0 1.0 CZ A:ARG96 4.4 33.7 1.0 S3A A:ICS502 4.4 64.1 1.0 O5 A:HCA501 4.7 51.0 1.0 NH2 A:ARG359 4.7 45.9 1.0 O7 A:HCA501 4.9 52.8 1.0

Iron binding site 8 out of 32 in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:53.1 occ:1.00 OE2 D:GLU109 2.1 33.0 1.0 O D:ARG108 2.3 23.9 1.0 OD2 B:ASP353 2.4 29.4 1.0 OD2 B:ASP357 2.5 28.5 1.0 O D:HOH942 2.7 23.1 1.0 OD1 B:ASP353 3.0 26.9 1.0 CG B:ASP353 3.1 24.6 1.0 CD D:GLU109 3.2 29.8 1.0 CG B:ASP357 3.3 25.6 1.0 OD1 B:ASP357 3.4 27.7 1.0 C D:ARG108 3.4 18.3 1.0 CG D:GLU109 3.7 25.7 1.0 N D:GLU109 4.2 19.5 1.0 CA D:GLU109 4.2 19.7 1.0 CB D:ARG108 4.2 16.4 1.0 OE1 D:GLU109 4.3 30.7 1.0 O D:HOH863 4.4 29.9 1.0 CD1 C:PHE429 4.4 22.3 1.0 CA D:ARG108 4.5 18.8 1.0 CB D:GLU109 4.5 23.2 1.0 CB B:ASP353 4.5 19.5 1.0 O D:PHE107 4.6 18.7 1.0 O B:ASP353 4.6 21.6 1.0 NZ C:LYS433 4.6 23.7 1.0 O B:HOH837 4.7 28.1 1.0 CB B:ASP357 4.8 23.5 1.0 O D:HOH856 4.8 26.7 1.0 CE1 C:PHE429 4.9 22.5 1.0 C B:ASP353 4.9 20.2 1.0 CG C:PHE429 5.0 22.9 1.0 O D:HOH975 5.0 28.4 1.0

Iron binding site 9 out of 32 in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe602 b:26.5 occ:1.00 FE1 B:CLF602 0.0 26.5 1.0 S2A B:CLF602 2.3 2.4 1.0 S3A B:CLF602 2.3 4.0 1.0 SG A:CYS154 2.4 15.5 1.0 S1 B:CLF602 2.4 11.8 1.0 FE2 B:CLF602 2.5 21.3 1.0 FE4 B:CLF602 2.6 30.3 1.0 FE3 B:CLF602 2.8 17.6 1.0 O B:HOH1004 3.5 20.4 1.0 CB A:CYS154 3.5 16.1 1.0 S4A B:CLF602 3.8 12.3 1.0 OG B:SER92 3.9 31.8 1.0 CA A:GLY185 3.9 11.3 1.0 SG B:CYS95 4.1 21.7 1.0 N A:CYS154 4.1 14.4 1.0 N A:GLY185 4.1 12.3 1.0 FE8 B:CLF602 4.4 24.6 1.0 CA A:CYS154 4.4 16.7 1.0 FE5 B:CLF602 4.6 40.9 1.0 C A:GLY185 4.7 17.2 1.0 CB B:SER92 4.8 25.7 1.0 SG A:CYS88 4.9 18.9 1.0 FE6 B:CLF602 4.9 42.9 1.0 N A:PHE186 4.9 17.6 1.0

Iron binding site 10 out of 32 in the Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Azotobacter Vinelandii Mofep (C1 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 1X Surfact within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe602 b:21.3 occ:1.00 FE2 B:CLF602 0.0 21.3 1.0 S4A B:CLF602 2.3 12.3 1.0 S2A B:CLF602 2.3 2.4 1.0 SG B:CYS95 2.3 21.7 1.0 S1 B:CLF602 2.5 11.8 1.0 FE1 B:CLF602 2.5 26.5 1.0 FE4 B:CLF602 2.6 30.3 1.0 FE3 B:CLF602 2.8 17.6 1.0 FE8 B:CLF602 3.0 24.6 1.0 N B:CYS95 3.2 16.9 1.0 CB B:CYS95 3.5 16.1 1.0 CA B:CYS95 3.5 15.3 1.0 S3A B:CLF602 3.8 4.0 1.0 FE5 B:CLF602 3.8 40.9 1.0 C B:GLY94 3.8 16.4 1.0 S4B B:CLF602 4.0 3.6 1.0 O B:HOH1004 4.2 20.4 1.0 OG B:SER92 4.2 31.8 1.0 CA B:GLY94 4.4 14.0 1.0 O B:GLY94 4.5 21.9 1.0 FE6 B:CLF602 4.6 42.9 1.0 SG A:CYS154 4.7 15.5 1.0 N B:GLY94 4.8 19.9 1.0 SG A:CYS88 4.8 18.9 1.0 SG A:CYS62 4.8 10.2 1.0 CB B:SER92 5.0 25.7 1.0

S.E.Enos, B.D.Cook, H.Rahmani, S.M.Narehood, Y.Li, I.C.Kuschnerus, T.H.Redford, P.Dukakis, D.Ji, M.J.Bachochin, D.A.Grotjahn, M.A.Herzik. A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle Cryoem. Biorxiv 2026.
ISSN: ISSN 2692-8205
PubMed: 41889805
DOI: 10.64898/2026.03.17.712260