Iron in PDB 7ut7: C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions

All present enzymatic activity of C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions:
1.18.6.1;

The structure of C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions (pdb code 7ut7). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 32 binding sites of Iron where determined in the C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions, PDB code: 7ut7:
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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:28.9 occ:1.00 FE1 A:ICS502 0.0 28.9 1.0 S2A A:ICS502 2.3 21.1 1.0 S4A A:ICS502 2.3 17.5 1.0 SG A:CYS275 2.3 23.6 1.0 S1A A:ICS502 2.3 18.0 1.0 FE4 A:ICS502 2.7 29.7 1.0 FE3 A:ICS502 2.7 32.3 1.0 FE2 A:ICS502 2.7 32.2 1.0 CB A:CYS275 3.2 17.6 1.0 CX A:ICS502 3.4 19.8 1.0 OG A:SER278 3.9 19.8 1.0 CB A:SER278 4.1 24.4 1.0 CB A:LEU358 4.2 20.7 1.0 CE2 A:TYR229 4.5 16.7 1.0 CA A:CYS275 4.5 25.5 1.0 N A:SER278 4.8 17.6 1.0 S2B A:ICS502 4.8 23.7 1.0 S5A A:ICS502 4.8 26.8 1.0 S3A A:ICS502 4.8 30.0 1.0 N A:LEU358 4.8 20.9 1.0 CD2 A:LEU358 4.9 23.8 1.0 FE7 A:ICS502 5.0 35.2 1.0 FE6 A:ICS502 5.0 30.3 1.0

Iron binding site 2 out of 32 in the C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:32.2 occ:1.00 FE2 A:ICS502 0.0 32.2 1.0 CX A:ICS502 2.0 19.8 1.0 S2B A:ICS502 2.2 23.7 1.0 S2A A:ICS502 2.2 21.1 1.0 S1A A:ICS502 2.3 18.0 1.0 FE6 A:ICS502 2.6 30.3 1.0 FE4 A:ICS502 2.7 29.7 1.0 FE3 A:ICS502 2.7 32.3 1.0 FE1 A:ICS502 2.7 28.9 1.0 FE5 A:ICS502 3.7 27.0 1.0 FE7 A:ICS502 3.7 35.2 1.0 S4A A:ICS502 3.9 17.5 1.0 CE1 A:HIS195 3.9 24.0 1.0 CZ A:PHE381 4.0 18.1 1.0 NE2 A:HIS195 4.0 20.1 1.0 S3B A:ICS502 4.2 26.0 1.0 S1B A:ICS502 4.2 28.9 1.0 CE1 A:PHE381 4.4 28.6 1.0 S3A A:ICS502 4.5 30.0 1.0 CG1 A:VAL70 4.5 16.0 1.0 S5A A:ICS502 4.5 26.8 1.0 SG A:CYS275 4.7 23.6 1.0 CG2 A:VAL70 4.8 19.9 1.0 N A:GLY357 4.8 24.2 1.0 CB A:SER278 5.0 24.4 1.0 ND1 A:HIS195 5.0 17.3 1.0

Iron binding site 3 out of 32 in the C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:32.3 occ:1.00 FE3 A:ICS502 0.0 32.3 1.0 CX A:ICS502 2.0 19.8 1.0 S5A A:ICS502 2.2 26.8 1.0 S4A A:ICS502 2.2 17.5 1.0 S2A A:ICS502 2.3 21.1 1.0 FE7 A:ICS502 2.6 35.2 1.0 FE4 A:ICS502 2.6 29.7 1.0 FE1 A:ICS502 2.7 28.9 1.0 FE2 A:ICS502 2.7 32.2 1.0 FE6 A:ICS502 3.7 30.3 1.0 FE5 A:ICS502 3.7 27.0 1.0 S1A A:ICS502 3.8 18.0 1.0 O A:HOH675 3.9 24.8 1.0 NH2 A:ARG96 4.0 27.2 1.0 CD2 A:TYR229 4.1 23.1 1.0 S3B A:ICS502 4.2 26.0 1.0 S4B A:ICS502 4.2 23.7 1.0 CE2 A:TYR229 4.3 16.7 1.0 S2B A:ICS502 4.5 23.7 1.0 S3A A:ICS502 4.5 30.0 1.0 SG A:CYS275 4.8 23.6 1.0

Iron binding site 4 out of 32 in the C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:29.7 occ:1.00 FE4 A:ICS502 0.0 29.7 1.0 CX A:ICS502 2.0 19.8 1.0 S3A A:ICS502 2.2 30.0 1.0 S1A A:ICS502 2.3 18.0 1.0 S4A A:ICS502 2.3 17.5 1.0 FE5 A:ICS502 2.6 27.0 1.0 FE3 A:ICS502 2.6 32.3 1.0 FE1 A:ICS502 2.7 28.9 1.0 FE2 A:ICS502 2.7 32.2 1.0 FE7 A:ICS502 3.7 35.2 1.0 FE6 A:ICS502 3.7 30.3 1.0 N A:LEU358 3.8 20.9 1.0 S2A A:ICS502 3.8 21.1 1.0 N A:GLY357 3.9 24.2 1.0 CB A:LEU358 4.1 20.7 1.0 S4B A:ICS502 4.2 23.7 1.0 S1B A:ICS502 4.3 28.9 1.0 S5A A:ICS502 4.5 26.8 1.0 CA A:LEU358 4.5 23.9 1.0 S2B A:ICS502 4.5 23.7 1.0 CA A:GLY357 4.5 20.1 1.0 N A:ARG359 4.6 16.7 1.0 C A:GLY357 4.6 20.9 1.0 SG A:CYS275 4.6 23.6 1.0 CG A:ARG359 4.8 24.0 1.0 C A:GLY356 4.9 23.1 1.0 CD A:ARG359 4.9 24.2 1.0 CA A:GLY356 4.9 17.4 1.0 CZ A:PHE381 5.0 18.1 1.0 NE A:ARG359 5.0 29.5 1.0

Iron binding site 5 out of 32 in the C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:27.0 occ:1.00 FE5 A:ICS502 0.0 27.0 1.0 CX A:ICS502 2.0 19.8 1.0 S4B A:ICS502 2.2 23.7 1.0 S3A A:ICS502 2.3 30.0 1.0 S1B A:ICS502 2.3 28.9 1.0 FE4 A:ICS502 2.6 29.7 1.0 FE7 A:ICS502 2.6 35.2 1.0 FE6 A:ICS502 2.6 30.3 1.0 MO1 A:ICS502 2.7 38.4 1.0 FE2 A:ICS502 3.7 32.2 1.0 FE3 A:ICS502 3.7 32.3 1.0 S3B A:ICS502 3.9 26.0 1.0 N A:GLY356 4.1 17.1 1.0 CA A:GLY356 4.1 17.4 1.0 ND1 A:HIS442 4.1 27.3 1.0 S1A A:ICS502 4.3 18.0 1.0 CG2 A:ILE355 4.3 18.8 1.0 S4A A:ICS502 4.3 17.5 1.0 S2B A:ICS502 4.5 23.7 1.0 S5A A:ICS502 4.5 26.8 1.0 N A:GLY357 4.5 24.2 1.0 CD A:ARG359 4.5 24.2 1.0 CE1 A:HIS442 4.5 17.6 1.0 NE A:ARG359 4.8 29.5 1.0 C A:GLY356 4.9 23.1 1.0 CG A:HIS442 4.9 23.5 1.0 CZ A:PHE381 5.0 18.1 1.0

Iron binding site 6 out of 32 in the C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:30.3 occ:1.00 FE6 A:ICS502 0.0 30.3 1.0 CX A:ICS502 2.0 19.8 1.0 S2B A:ICS502 2.2 23.7 1.0 S3B A:ICS502 2.2 26.0 1.0 S1B A:ICS502 2.2 28.9 1.0 FE2 A:ICS502 2.6 32.2 1.0 FE7 A:ICS502 2.6 35.2 1.0 FE5 A:ICS502 2.6 27.0 1.0 MO1 A:ICS502 2.7 38.4 1.0 FE3 A:ICS502 3.7 32.3 1.0 FE4 A:ICS502 3.7 29.7 1.0 S4B A:ICS502 3.8 23.7 1.0 O7 A:HCA501 4.1 25.5 1.0 CZ A:PHE381 4.1 18.1 1.0 O1 A:HCA501 4.2 32.5 1.0 S2A A:ICS502 4.2 21.1 1.0 S1A A:ICS502 4.3 18.0 1.0 CG2 A:VAL70 4.4 19.9 1.0 S5A A:ICS502 4.5 26.8 1.0 S3A A:ICS502 4.5 30.0 1.0 CE2 A:PHE381 4.7 20.9 1.0 O5 A:HCA501 4.8 14.7 1.0 ND1 A:HIS442 5.0 27.3 1.0 FE1 A:ICS502 5.0 28.9 1.0

Iron binding site 7 out of 32 in the C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:35.2 occ:1.00 FE7 A:ICS502 0.0 35.2 1.0 CX A:ICS502 2.0 19.8 1.0 S5A A:ICS502 2.2 26.8 1.0 S4B A:ICS502 2.2 23.7 1.0 S3B A:ICS502 2.2 26.0 1.0 FE3 A:ICS502 2.6 32.3 1.0 FE6 A:ICS502 2.6 30.3 1.0 FE5 A:ICS502 2.6 27.0 1.0 MO1 A:ICS502 2.7 38.4 1.0 FE2 A:ICS502 3.7 32.2 1.0 FE4 A:ICS502 3.7 29.7 1.0 S1B A:ICS502 3.8 28.9 1.0 O A:HOH619 3.9 22.5 1.0 NE A:ARG96 4.1 19.7 1.0 NH2 A:ARG96 4.1 27.2 1.0 O5 A:HCA501 4.2 14.7 1.0 S2A A:ICS502 4.3 21.1 1.0 S4A A:ICS502 4.3 17.5 1.0 S2B A:ICS502 4.4 23.7 1.0 S3A A:ICS502 4.5 30.0 1.0 CZ A:ARG96 4.6 13.7 1.0 CZ A:ARG359 4.6 25.9 1.0 NH2 A:ARG359 4.8 22.9 1.0 NE A:ARG359 4.8 29.5 1.0 NH1 A:ARG359 4.9 17.1 1.0 FE1 A:ICS502 5.0 28.9 1.0

Iron binding site 8 out of 32 in the C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:23.9 occ:1.00 O D:HOH812 2.2 18.8 1.0 OE1 D:GLU109 2.2 25.1 1.0 O D:ARG108 2.3 17.8 1.0 OD2 B:ASP353 2.3 29.6 1.0 O B:HOH755 2.4 21.8 1.0 OD2 B:ASP357 2.4 22.8 1.0 CG B:ASP353 3.0 16.6 1.0 OD1 B:ASP353 3.0 23.2 1.0 CD D:GLU109 3.2 22.6 1.0 C D:ARG108 3.4 8.1 1.0 CG B:ASP357 3.4 16.5 1.0 CG D:GLU109 3.7 14.8 1.0 OD1 B:ASP357 3.7 23.4 1.0 CB D:ARG108 4.1 13.3 1.0 CA D:GLU109 4.2 13.4 1.0 N D:GLU109 4.2 15.0 1.0 OE2 D:GLU109 4.3 29.5 1.0 CA D:ARG108 4.4 13.6 1.0 NZ C:LYS433 4.4 24.2 1.0 O D:HOH738 4.4 28.5 1.0 O D:HOH830 4.4 25.8 1.0 CB B:ASP353 4.4 14.1 1.0 CD1 C:PHE429 4.5 20.0 1.0 O D:PHE107 4.5 21.8 1.0 CB D:GLU109 4.5 13.5 1.0 CE C:LYS433 4.6 24.7 1.0 O B:ASP353 4.6 21.4 1.0 O D:HOH794 4.7 23.3 1.0 CB B:ASP357 4.8 16.0 1.0 C B:ASP353 4.9 11.8 1.0 CE1 C:PHE429 4.9 19.0 1.0 CG C:PHE429 5.0 18.4 1.0

Iron binding site 9 out of 32 in the C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe602 b:28.8 occ:1.00 FE1 B:CLF602 0.0 28.8 1.0 S3A B:CLF602 2.3 20.4 1.0 S2A B:CLF602 2.3 15.8 1.0 SG B:CYS95 2.3 19.1 1.0 S1 B:CLF602 2.5 16.8 1.0 FE2 B:CLF602 2.5 29.4 1.0 FE4 B:CLF602 2.6 28.4 1.0 FE3 B:CLF602 2.7 23.5 1.0 FE8 B:CLF602 2.9 25.1 1.0 N B:CYS95 3.1 4.6 1.0 CB B:CYS95 3.4 5.9 1.0 CA B:CYS95 3.4 8.1 1.0 S4A B:CLF602 3.7 16.8 1.0 C B:GLY94 3.8 9.3 1.0 S4B B:CLF602 4.0 19.8 1.0 CA B:GLY94 4.4 10.5 1.0 O B:HOH776 4.4 17.1 1.0 SG A:CYS154 4.5 18.1 1.0 O B:GLY94 4.6 14.4 1.0 SG A:CYS62 4.7 15.8 1.0 CB B:SER92 4.7 16.4 1.0 FE5 B:CLF602 4.8 39.5 1.0 N B:GLY94 4.8 12.4 1.0 OG B:SER92 4.8 25.8 1.0 O B:SER92 4.9 19.9 1.0 SG A:CYS88 4.9 17.2 1.0 C B:CYS95 4.9 6.7 1.0

Iron binding site 10 out of 32 in the C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep 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 C2 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe602 b:29.4 occ:1.00 FE2 B:CLF602 0.0 29.4 1.0 S2A B:CLF602 2.3 15.8 1.0 SG A:CYS154 2.3 18.1 1.0 S4A B:CLF602 2.3 16.8 1.0 S1 B:CLF602 2.4 16.8 1.0 FE1 B:CLF602 2.5 28.8 1.0 FE4 B:CLF602 2.6 28.4 1.0 FE3 B:CLF602 2.8 23.5 1.0 CB A:CYS154 3.5 10.6 1.0 O B:HOH776 3.7 17.1 1.0 S3A B:CLF602 3.8 20.4 1.0 CA A:GLY185 3.8 13.7 1.0 N A:CYS154 4.0 19.1 1.0 N A:GLY185 4.1 23.3 1.0 SG B:CYS95 4.1 19.1 1.0 OG B:SER92 4.3 25.8 1.0 CA A:CYS154 4.3 16.7 1.0 FE8 B:CLF602 4.4 25.1 1.0 C A:GLY185 4.5 19.6 1.0 CB B:SER92 4.6 16.4 1.0 N A:PHE186 4.8 22.5 1.0 SG A:CYS62 4.9 15.8 1.0 SG A:CYS88 4.9 17.2 1.0

H.L.Rutledge, B.D.Cook, H.P.M.Nguyen, M.A.Herzik Jr., F.A.Tezcan. Structures of the Nitrogenase Complex Prepared Under Catalytic Turnover Conditions. Science V. 377 865 2022.
ISSN: ESSN 1095-9203
PubMed: 35901182
DOI: 10.1126/SCIENCE.ABQ7641