Iron in PDB 8e3u: Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation

All present enzymatic activity of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation:
1.18.6.1;

The structure of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation, PDB code: 8e3u was solved by H.L.Rutledge, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.89 / 1.99
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	77.259, 129.009, 107.76, 90, 109.22, 90
R / Rfree (%)	20.2 / 25.3

The structure of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation also contains other interesting chemical elements:

Sodium	(Na)	2 atoms
Molybdenum	(Mo)	2 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30;

Binding sites:

The binding sites of Iron atom in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation (pdb code 8e3u). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 30 binding sites of Iron where determined in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation, PDB code: 8e3u:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 30 in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:33.4 occ:0.73 FE2 A:UFF601 0.0 33.4 0.7 S2A A:UFF601 2.1 34.8 1.0 SG A:CYS154 2.2 31.0 1.0 S4A A:UFF601 2.4 27.8 1.0 S1 A:UFF601 2.5 32.6 1.0 FE4 A:UFF601 2.7 31.6 0.7 H A:CYS154 2.7 48.8 1.0 FE3 A:UFF601 2.8 32.2 0.8 HB2 A:CYS154 2.9 44.8 1.0 NA B:NA602 3.0 25.5 0.7 HA3 A:GLY185 3.1 47.7 1.0 CB A:CYS154 3.1 37.4 1.0 HG B:SER92 3.3 61.4 1.0 N A:CYS154 3.6 40.7 1.0 H A:GLY185 3.7 50.0 1.0 S3A A:UFF601 3.7 40.5 1.0 CA A:CYS154 3.9 38.8 1.0 O B:HOH759 3.9 26.7 1.0 CA A:GLY185 4.0 39.7 1.0 HB3 A:CYS154 4.0 44.8 1.0 OG B:SER92 4.0 51.2 1.0 HA A:CYS154 4.1 46.6 1.0 SG B:CYS95 4.2 29.0 1.0 N A:GLY185 4.3 41.6 1.0 FE8 A:UFF601 4.3 34.5 0.8 HB3 A:GLU153 4.4 36.5 1.0 HD3 A:PRO155 4.4 54.3 1.0 FE5 A:UFF601 4.5 32.5 0.5 HA2 A:GLY185 4.5 47.7 1.0 SG A:CYS88 4.7 29.2 1.0 SG B:CYS153 4.7 38.3 1.0 HA A:GLU153 4.7 45.9 1.0 HB2 B:SER92 4.7 44.2 1.0 C A:GLY185 4.8 39.9 1.0 C A:GLU153 4.8 38.2 1.0 FE6 A:UFF601 4.8 30.9 1.0 HB2 B:MET154 4.9 42.2 1.0 SG A:CYS62 4.9 36.2 1.0 H A:PHE186 4.9 54.0 1.0 CB B:SER92 4.9 36.8 1.0 HB3 A:TYR64 5.0 40.6 1.0

Iron binding site 2 out of 30 in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:32.2 occ:0.83 FE3 A:UFF601 0.0 32.2 0.8 S3A A:UFF601 2.0 40.5 1.0 S2A A:UFF601 2.1 34.8 1.0 S4A A:UFF601 2.2 27.8 1.0 SG A:CYS62 2.3 36.2 1.0 FE4 A:UFF601 2.5 31.6 0.7 FE2 A:UFF601 2.8 33.4 0.7 HB3 A:TYR64 2.9 40.6 1.0 NA B:NA602 3.1 25.5 0.7 HA3 A:GLY185 3.1 47.7 1.0 HG A:CYS62 3.3 43.5 1.0 CB A:CYS62 3.6 36.2 1.0 HB2 A:CYS62 3.6 43.4 1.0 HA3 B:GLY94 3.7 41.3 1.0 HD1 A:TYR64 3.8 43.1 1.0 HB3 A:CYS62 3.8 43.4 1.0 HA2 A:GLY185 3.8 47.7 1.0 CA A:GLY185 3.9 39.7 1.0 CB A:TYR64 4.0 33.8 1.0 H A:TYR64 4.1 36.8 1.0 HE2 B:TYR98 4.1 40.6 1.0 S1 A:UFF601 4.2 32.6 1.0 HB2 A:TYR64 4.3 40.6 1.0 H A:GLY185 4.3 50.0 1.0 HB3 A:CYS88 4.3 38.5 1.0 CD1 A:TYR64 4.3 35.9 1.0 CG A:TYR64 4.5 33.5 1.0 H A:CYS154 4.5 48.8 1.0 H A:ALA65 4.5 33.2 1.0 N A:GLY185 4.6 41.6 1.0 SG A:CYS154 4.6 31.0 1.0 H B:CYS95 4.7 31.3 1.0 CA B:GLY94 4.7 34.4 1.0 SG A:CYS88 4.7 29.2 1.0 N B:CYS95 4.8 26.1 1.0 HD2 B:TYR98 4.9 29.6 1.0 C B:GLY94 4.9 32.3 1.0 N A:TYR64 4.9 30.6 1.0 CE2 B:TYR98 4.9 33.8 1.0 CA A:CYS62 4.9 29.6 1.0 HG B:SER92 5.0 61.4 1.0 SG B:CYS95 5.0 29.0 1.0 C A:GLY185 5.0 39.9 1.0 CA A:TYR64 5.0 30.6 1.0

Iron binding site 3 out of 30 in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:31.6 occ:0.68 FE4 A:UFF601 0.0 31.6 0.7 S3A A:UFF601 2.1 40.5 1.0 SG A:CYS88 2.3 29.2 1.0 S4A A:UFF601 2.4 27.8 1.0 S1 A:UFF601 2.5 32.6 1.0 FE3 A:UFF601 2.5 32.2 0.8 NA B:NA602 2.5 25.5 0.7 FE2 A:UFF601 2.7 33.4 0.7 FE5 A:UFF601 2.8 32.5 0.5 HB3 A:CYS88 3.0 38.5 1.0 CB A:CYS88 3.3 32.1 1.0 S2A A:UFF601 3.5 34.8 1.0 HG2 A:GLU153 3.6 45.0 1.0 H A:CYS154 3.8 48.8 1.0 HB3 A:GLU153 3.8 36.5 1.0 FE8 A:UFF601 3.9 34.5 0.8 HB2 A:CYS88 4.0 38.5 1.0 HA A:CYS88 4.1 44.9 1.0 H A:CYS88 4.1 33.3 1.0 CA A:CYS88 4.3 37.4 1.0 HB3 A:TYR64 4.3 40.6 1.0 S2B A:UFF601 4.3 24.5 1.0 S4B A:UFF601 4.3 29.4 1.0 CG A:GLU153 4.5 37.5 1.0 HE2 B:TYR98 4.5 40.6 1.0 HA A:GLU153 4.5 45.9 1.0 FE6 A:UFF601 4.5 30.9 1.0 CB A:GLU153 4.6 30.4 1.0 HD1 A:TYR64 4.6 43.1 1.0 SG B:CYS95 4.6 29.0 1.0 N A:CYS88 4.6 27.7 1.0 CD1 A:TYR64 4.7 35.9 1.0 HB2 A:CYS154 4.7 44.8 1.0 SG A:CYS62 4.7 36.2 1.0 N A:CYS154 4.8 40.7 1.0 HA3 A:GLY185 4.8 47.7 1.0 HD2 B:TYR98 4.8 29.6 1.0 CG A:TYR64 4.9 33.5 1.0 SG A:CYS154 4.9 31.0 1.0 CD A:GLU153 4.9 38.3 1.0 CB A:TYR64 5.0 33.8 1.0

Iron binding site 4 out of 30 in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:32.5 occ:0.51 FE5 A:UFF601 0.0 32.5 0.5 S2B A:UFF601 1.7 24.5 1.0 S4B A:UFF601 2.1 29.4 1.0 SG A:CYS88 2.3 29.2 1.0 S1 A:UFF601 2.3 32.6 1.0 FE8 A:UFF601 2.3 34.5 0.8 FE6 A:UFF601 2.6 30.9 1.0 H A:CYS88 2.7 33.3 1.0 FE4 A:UFF601 2.8 31.6 0.7 FE7 A:UFF601 2.9 29.1 1.0 NA B:NA602 3.1 25.5 0.7 N A:CYS88 3.3 27.7 1.0 HA3 A:GLY87 3.5 42.5 1.0 CB A:CYS88 3.7 32.1 1.0 S3B A:UFF601 3.7 31.3 1.0 S3A A:UFF601 3.8 40.5 1.0 HA A:CYS88 3.9 44.9 1.0 CA A:CYS88 3.9 37.4 1.0 C A:GLY87 4.1 31.2 1.0 HB3 A:CYS88 4.2 38.5 1.0 CA A:GLY87 4.2 35.4 1.0 SG B:CYS95 4.2 29.0 1.0 H A:GLY87 4.4 35.0 1.0 HE2 A:TYR91 4.4 29.5 1.0 FE2 A:UFF601 4.5 33.4 0.7 HB2 A:CYS88 4.5 38.5 1.0 SG B:CYS153 4.6 38.3 1.0 HB2 A:PRO85 4.6 34.9 1.0 N A:GLY87 4.7 29.1 1.0 HB3 A:GLU153 4.8 36.5 1.0 HA B:CYS95 4.8 39.3 1.0 SG B:CYS70 4.8 25.2 1.0 HD2 A:TYR91 4.8 39.5 1.0 OE1 A:GLU153 5.0 48.4 1.0 HD2 A:PRO85 5.0 32.5 1.0 HB3 B:CYS95 5.0 43.7 1.0

Iron binding site 5 out of 30 in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:30.9 occ:0.97 FE6 A:UFF601 0.0 30.9 1.0 SG B:CYS153 2.3 38.3 1.0 S3B A:UFF601 2.3 31.3 1.0 S2B A:UFF601 2.4 24.5 1.0 S1 A:UFF601 2.4 32.6 1.0 FE5 A:UFF601 2.6 32.5 0.5 FE8 A:UFF601 2.7 34.5 0.8 FE7 A:UFF601 2.9 29.1 1.0 H B:CYS153 3.0 42.1 1.0 HB3 B:CYS153 3.1 30.3 1.0 CB B:CYS153 3.3 25.2 1.0 HB2 B:ALA188 3.4 35.7 1.0 HB3 B:ALA188 3.5 35.7 1.0 HG2 A:PRO85 3.5 39.5 1.0 HB2 A:PRO85 3.7 34.9 1.0 CB B:ALA188 3.8 29.7 1.0 HB1 B:ALA188 3.8 35.7 1.0 S4B A:UFF601 3.8 29.4 1.0 N B:CYS153 3.9 35.1 1.0 HD2 A:PRO85 4.0 32.5 1.0 HB2 B:CYS153 4.1 30.3 1.0 CA B:CYS153 4.2 39.0 1.0 SG A:CYS88 4.3 29.2 1.0 CG A:PRO85 4.4 32.9 1.0 HB B:THR152 4.4 35.7 1.0 HB2 A:CYS154 4.4 44.8 1.0 CB A:PRO85 4.5 29.1 1.0 NA B:NA602 4.5 25.5 0.7 FE4 A:UFF601 4.5 31.6 0.7 HD3 A:PRO155 4.6 54.3 1.0 SG B:CYS95 4.6 29.0 1.0 H A:CYS88 4.6 33.3 1.0 O B:HOH823 4.7 29.8 1.0 CD A:PRO85 4.7 27.1 1.0 HA3 A:GLY87 4.8 42.5 1.0 FE2 A:UFF601 4.8 33.4 0.7 O B:HOH759 4.8 26.7 1.0 H A:GLY87 4.9 35.0 1.0 HA B:THR152 4.9 33.2 1.0 H B:MET154 4.9 45.1 1.0 HA B:CYS153 4.9 46.8 1.0 HG3 A:PRO155 5.0 49.5 1.0 HB3 A:GLU153 5.0 36.5 1.0 SG B:CYS70 5.0 25.2 1.0

Iron binding site 6 out of 30 in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:29.1 occ:1.00 FE7 A:UFF601 0.0 29.1 1.0 SG B:CYS70 2.2 25.2 1.0 S4B A:UFF601 2.2 29.4 1.0 S2B A:UFF601 2.2 24.5 1.0 S3B A:UFF601 2.5 31.3 1.0 FE8 A:UFF601 2.8 34.5 0.8 HA3 A:GLY87 2.9 42.5 1.0 FE6 A:UFF601 2.9 30.9 1.0 FE5 A:UFF601 2.9 32.5 0.5 HB2 B:ALA188 3.1 35.7 1.0 CB B:CYS70 3.3 27.2 1.0 HB2 B:CYS70 3.4 32.7 1.0 HB3 B:CYS70 3.4 32.7 1.0 HE2 A:TYR91 3.4 29.5 1.0 HB1 B:ALA188 3.6 35.7 1.0 HG2 B:PRO72 3.7 29.2 1.0 CB B:ALA188 3.8 29.7 1.0 HZ B:PHE99 3.9 34.3 1.0 HE1 B:PHE99 3.9 33.5 1.0 CA A:GLY87 3.9 35.4 1.0 HD2 B:PRO72 4.0 38.6 1.0 H A:GLY87 4.1 35.0 1.0 HH A:TYR91 4.1 29.5 1.0 HB3 B:ALA188 4.2 35.7 1.0 S1 A:UFF601 4.2 32.6 1.0 HG3 B:PRO72 4.3 29.2 1.0 H A:CYS88 4.3 33.3 1.0 CG B:PRO72 4.3 24.3 1.0 CE2 A:TYR91 4.4 24.6 1.0 HB2 A:PRO85 4.4 34.9 1.0 HB3 B:CYS95 4.4 43.7 1.0 HA2 A:GLY87 4.4 42.5 1.0 N A:GLY87 4.5 29.1 1.0 CZ B:PHE99 4.6 28.6 1.0 CE1 B:PHE99 4.6 27.9 1.0 H B:CYS70 4.6 27.2 1.0 H B:CYS153 4.7 42.1 1.0 CA B:CYS70 4.7 24.5 1.0 CD B:PRO72 4.7 32.1 1.0 C A:GLY87 4.7 31.2 1.0 N A:CYS88 4.7 27.7 1.0 SG B:CYS95 4.8 29.0 1.0 OH A:TYR91 4.9 24.6 1.0 HB3 B:CYS153 4.9 30.3 1.0 HA B:ALA188 4.9 32.2 1.0 NA B:NA602 5.0 25.5 0.7 SG A:CYS88 5.0 29.2 1.0 HA B:THR152 5.0 33.2 1.0

Iron binding site 7 out of 30 in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:34.5 occ:0.84 FE8 A:UFF601 0.0 34.5 0.8 SG B:CYS95 2.2 29.0 1.0 S1 A:UFF601 2.2 32.6 1.0 S3B A:UFF601 2.2 31.3 1.0 S4B A:UFF601 2.3 29.4 1.0 FE5 A:UFF601 2.3 32.5 0.5 NA B:NA602 2.4 25.5 0.7 FE6 A:UFF601 2.7 30.9 1.0 FE7 A:UFF601 2.8 29.1 1.0 HB3 B:CYS95 3.0 43.7 1.0 CB B:CYS95 3.2 36.4 1.0 S2B A:UFF601 3.3 24.5 1.0 HB B:THR152 3.5 35.7 1.0 HA B:CYS95 3.7 39.3 1.0 H B:CYS153 3.8 42.1 1.0 FE4 A:UFF601 3.9 31.6 0.7 HZ B:PHE99 3.9 34.3 1.0 CA B:CYS95 4.0 32.8 1.0 HB2 B:CYS95 4.1 43.7 1.0 S3A A:UFF601 4.2 40.5 1.0 FE2 A:UFF601 4.3 33.4 0.7 SG B:CYS153 4.4 38.3 1.0 SG A:CYS88 4.4 29.2 1.0 HA B:THR152 4.5 33.2 1.0 H B:CYS95 4.5 31.3 1.0 CB B:THR152 4.5 29.7 1.0 HE1 B:PHE99 4.6 33.5 1.0 CZ B:PHE99 4.6 28.6 1.0 HG22 B:THR152 4.7 34.2 1.0 N B:CYS95 4.7 26.1 1.0 O B:HOH759 4.7 26.7 1.0 HE2 A:TYR91 4.7 29.5 1.0 SG B:CYS70 4.8 25.2 1.0 S2A A:UFF601 4.8 34.8 1.0 N B:CYS153 4.8 35.1 1.0 HA3 A:GLY87 4.8 42.5 1.0 HG21 B:THR152 4.9 34.2 1.0 H A:CYS88 4.9 33.3 1.0 HB2 B:ALA188 5.0 35.7 1.0 HG2 B:PRO72 5.0 29.2 1.0 CG2 B:THR152 5.0 28.5 1.0 CE1 B:PHE99 5.0 27.9 1.0

Iron binding site 8 out of 30 in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe603 b:30.9 occ:1.00 FE1 A:ICS603 0.0 30.9 1.0 S2A A:ICS603 2.3 28.3 1.0 S1A A:ICS603 2.3 39.5 1.0 S4A A:ICS603 2.3 27.8 1.0 SG A:CYS275 2.3 38.6 1.0 FE2 A:ICS603 2.6 30.3 1.0 FE4 A:ICS603 2.7 33.6 1.0 FE3 A:ICS603 2.7 28.3 1.0 HB2 A:CYS275 3.2 41.5 1.0 HG A:SER278 3.3 34.2 1.0 CB A:CYS275 3.4 34.5 1.0 HB3 A:SER278 3.4 47.9 1.0 CX A:ICS603 3.5 26.3 1.0 HB3 A:LEU358 3.7 45.2 1.0 HE2 A:TYR229 3.8 35.6 1.0 HB3 A:CYS275 3.8 41.5 1.0 OG A:SER278 3.9 28.5 1.0 HB2 A:LEU358 3.9 45.2 1.0 HD22 A:LEU358 4.1 51.8 1.0 CB A:SER278 4.1 39.9 1.0 H A:SER278 4.2 37.5 1.0 CB A:LEU358 4.3 37.7 1.0 CE2 A:TYR229 4.5 29.6 1.0 HD23 A:LEU358 4.5 51.8 1.0 HB3 A:ARG277 4.6 51.4 1.0 HA A:CYS275 4.6 51.7 1.0 CA A:CYS275 4.6 43.1 1.0 HE1 A:HIS195 4.7 43.5 1.0 S2B A:ICS603 4.7 31.6 1.0 CD2 A:LEU358 4.7 43.1 1.0 HD2 A:TYR229 4.7 34.7 1.0 HB2 A:SER278 4.7 47.9 1.0 S3A A:ICS603 4.8 28.4 1.0 N A:SER278 4.9 31.3 1.0 S5A A:ICS603 4.9 24.8 1.0 HA3 A:GLY357 4.9 45.4 1.0 FE6 A:ICS603 5.0 33.5 1.0 HH A:TYR229 5.0 41.7 1.0 CD2 A:TYR229 5.0 28.9 1.0

Iron binding site 9 out of 30 in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe603 b:30.3 occ:1.00 FE2 A:ICS603 0.0 30.3 1.0 CX A:ICS603 2.0 26.3 1.0 S2B A:ICS603 2.2 31.6 1.0 S1A A:ICS603 2.3 39.5 1.0 S2A A:ICS603 2.3 28.3 1.0 FE6 A:ICS603 2.6 33.5 1.0 FE1 A:ICS603 2.6 30.9 1.0 FE3 A:ICS603 2.7 28.3 1.0 FE4 A:ICS603 2.7 33.6 1.0 HZ A:PHE381 3.5 45.3 1.0 HE1 A:HIS195 3.5 43.5 1.0 FE5 A:ICS603 3.7 34.9 1.0 FE7 A:ICS603 3.7 24.3 1.0 S4A A:ICS603 3.8 27.8 1.0 HE1 A:PHE381 4.0 52.6 1.0 HB3 A:SER278 4.0 47.9 1.0 HE2 A:HIS195 4.1 53.3 1.0 S3B A:ICS603 4.1 28.5 1.0 CE1 A:HIS195 4.2 36.3 1.0 S1B A:ICS603 4.3 31.0 1.0 HG21 A:VAL70 4.3 54.4 1.0 NE2 A:HIS195 4.4 44.4 1.0 CZ A:PHE381 4.4 37.8 1.0 S5A A:ICS603 4.5 24.8 1.0 HB A:VAL70 4.5 52.7 1.0 S3A A:ICS603 4.5 28.4 1.0 CE1 A:PHE381 4.6 43.8 1.0 HG11 A:VAL70 4.7 47.5 1.0 H A:GLY357 4.7 38.6 1.0 SG A:CYS275 4.7 38.6 1.0 HA3 A:GLY357 4.9 45.4 1.0 CB A:SER278 4.9 39.9 1.0 HH11 A:ARG96 4.9 39.5 1.0 HG A:SER278 4.9 34.2 1.0 CG2 A:VAL70 5.0 45.3 1.0 HG23 A:VAL70 5.0 54.4 1.0

Iron binding site 10 out of 30 in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe603 b:28.3 occ:1.00 FE3 A:ICS603 0.0 28.3 1.0 CX A:ICS603 2.0 26.3 1.0 S5A A:ICS603 2.2 24.8 1.0 S4A A:ICS603 2.3 27.8 1.0 S2A A:ICS603 2.3 28.3 1.0 FE2 A:ICS603 2.7 30.3 1.0 FE7 A:ICS603 2.7 24.3 1.0 FE4 A:ICS603 2.7 33.6 1.0 FE1 A:ICS603 2.7 30.9 1.0 HD2 A:TYR229 3.7 34.7 1.0 FE6 A:ICS603 3.7 33.5 1.0 HH12 A:ARG96 3.8 39.5 1.0 FE5 A:ICS603 3.8 34.9 1.0 HH11 A:ARG96 3.9 39.5 1.0 S1A A:ICS603 3.9 39.5 1.0 S3B A:ICS603 4.1 28.5 1.0 CD2 A:TYR229 4.2 28.9 1.0 NH1 A:ARG96 4.2 32.9 1.0 HE2 A:TYR229 4.2 35.6 1.0 S4B A:ICS603 4.3 33.9 1.0 O A:HOH846 4.3 39.0 1.0 CE2 A:TYR229 4.5 29.6 1.0 S2B A:ICS603 4.5 31.6 1.0 S3A A:ICS603 4.5 28.4 1.0 HB2 A:CYS275 4.7 41.5 1.0 HH21 A:ARG359 4.8 30.8 1.0 HE A:ARG359 4.8 44.5 1.0 HB2 A:TYR229 4.8 30.7 1.0 SG A:CYS275 4.9 38.6 1.0 NH2 A:ARG359 5.0 25.6 1.0 NE A:ARG359 5.0 37.1 1.0

H.L.Rutledge, M.J.Field, J.Rittle, M.T.Green, F.A.Tezcan. Role of Serine Coordination in the Structural and Functional Protection of the Nitrogenase P-Cluster. J.Am.Chem.Soc. V. 144 22101 2022.
ISSN: ESSN 1520-5126
PubMed: 36445204
DOI: 10.1021/JACS.2C09480