Iron in PDB 6o7q: Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling

All present enzymatic activity of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling:
1.18.6.1;

The structure of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling, PDB code: 6o7q 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)	48.68 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	77.437, 130.413, 107.751, 90.00, 109.09, 90.00
R / Rfree (%)	18.6 / 22.9

The structure of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling 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 Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling (pdb code 6o7q). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 32 binding sites of Iron where determined in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling, PDB code: 6o7q:
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 Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:26.8 occ:1.00 FE1 A:CLF501 0.0 26.8 1.0 S3A A:CLF501 2.3 17.7 1.0 S2A A:CLF501 2.3 18.9 1.0 S1 A:CLF501 2.5 21.6 1.0 SG B:CYS95 2.5 16.4 1.0 FE4 A:CLF501 2.6 27.7 1.0 FE2 A:CLF501 2.6 26.4 1.0 FE3 A:CLF501 2.8 31.9 1.0 FE8 A:CLF501 2.9 33.0 1.0 H B:CYS95 3.1 27.9 1.0 HA B:CYS95 3.3 27.2 1.0 N B:CYS95 3.3 23.2 1.0 CB B:CYS95 3.5 21.8 1.0 CA B:CYS95 3.6 22.7 1.0 S4A A:CLF501 3.8 16.9 1.0 FE5 A:CLF501 3.8 30.3 1.0 S4B A:CLF501 3.8 20.0 1.0 C B:GLY94 3.9 25.8 1.0 HA3 B:GLY94 3.9 29.6 1.0 HB3 B:CYS95 3.9 26.2 1.0 HB2 B:CYS95 4.3 26.2 1.0 HD2 B:TYR98 4.4 27.5 1.0 CA B:GLY94 4.4 24.7 1.0 HB2 B:SER92 4.4 27.5 1.0 O B:HOH822 4.5 20.6 1.0 O B:GLY94 4.6 20.8 1.0 SG A:CYS88 4.6 20.7 1.0 HA3 A:GLY185 4.7 29.6 1.0 SG A:CYS154 4.7 19.4 1.0 H B:GLY94 4.8 27.1 1.0 SG A:CYS62 4.8 21.1 1.0 N B:GLY94 4.9 22.6 1.0 HB B:THR152 4.9 23.2 1.0 OG B:SER92 5.0 28.1 1.0

Iron binding site 2 out of 32 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:26.4 occ:1.00 FE2 A:CLF501 0.0 26.4 1.0 S2A A:CLF501 2.2 18.9 1.0 S4A A:CLF501 2.3 16.9 1.0 SG A:CYS154 2.4 19.4 1.0 S1 A:CLF501 2.5 21.6 1.0 FE1 A:CLF501 2.6 26.8 1.0 FE4 A:CLF501 2.6 27.7 1.0 FE3 A:CLF501 2.8 31.9 1.0 HA3 A:GLY185 2.9 29.6 1.0 HB2 A:CYS154 3.2 21.5 1.0 H A:CYS154 3.2 30.1 1.0 CB A:CYS154 3.4 17.9 1.0 H A:GLY185 3.6 34.9 1.0 O B:HOH822 3.8 20.6 1.0 S3A A:CLF501 3.8 17.7 1.0 CA A:GLY185 3.8 24.7 1.0 N A:CYS154 4.0 25.1 1.0 N A:GLY185 4.1 29.1 1.0 HB3 A:CYS154 4.2 21.5 1.0 SG B:CYS95 4.2 16.4 1.0 CA A:CYS154 4.2 23.8 1.0 HB2 B:SER92 4.2 27.5 1.0 OG B:SER92 4.2 28.1 1.0 HA A:CYS154 4.4 28.6 1.0 HA2 A:GLY185 4.4 29.6 1.0 FE8 A:CLF501 4.4 33.0 1.0 C A:GLY185 4.6 28.4 1.0 HB3 A:GLU153 4.6 24.0 1.0 CB B:SER92 4.7 22.9 1.0 HA A:GLU153 4.8 26.8 1.0 H A:PHE186 4.8 31.5 1.0 FE5 A:CLF501 4.8 30.3 1.0 SG A:CYS88 4.8 20.7 1.0 HG B:SER92 4.8 33.7 1.0 SG A:CYS62 4.9 21.1 1.0 N A:PHE186 4.9 26.3 1.0

Iron binding site 3 out of 32 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:31.9 occ:1.00 FE3 A:CLF501 0.0 31.9 1.0 S2A A:CLF501 2.3 18.9 1.0 S3A A:CLF501 2.3 17.7 1.0 S4A A:CLF501 2.3 16.9 1.0 SG A:CYS62 2.3 21.1 1.0 FE4 A:CLF501 2.7 27.7 1.0 FE2 A:CLF501 2.8 26.4 1.0 FE1 A:CLF501 2.8 26.8 1.0 HA3 A:GLY185 3.0 29.6 1.0 HB3 A:TYR64 3.0 24.4 1.0 CB A:CYS62 3.4 22.9 1.0 HB3 A:CYS62 3.4 27.5 1.0 HB2 A:CYS62 3.4 27.5 1.0 HA3 B:GLY94 3.5 29.6 1.0 HA2 A:GLY185 3.7 29.6 1.0 CA A:GLY185 3.8 24.7 1.0 CB A:TYR64 3.9 20.3 1.0 HB2 A:TYR64 4.0 24.4 1.0 HD1 A:TYR64 4.1 23.2 1.0 H A:TYR64 4.2 22.8 1.0 HE2 B:TYR98 4.2 25.9 1.0 S1 A:CLF501 4.2 21.6 1.0 H A:GLY185 4.3 34.9 1.0 CA B:GLY94 4.4 24.7 1.0 N A:GLY185 4.5 29.1 1.0 CG A:TYR64 4.5 22.6 1.0 CD1 A:TYR64 4.5 19.4 1.0 C B:GLY94 4.6 25.8 1.0 H A:ALA65 4.6 21.6 1.0 HB3 A:CYS88 4.7 29.1 1.0 H B:CYS95 4.7 27.9 1.0 O B:HOH1007 4.7 23.0 1.0 N B:CYS95 4.8 23.2 1.0 CA A:CYS62 4.8 23.5 1.0 SG A:CYS154 4.8 19.4 1.0 C A:GLY185 4.8 28.4 1.0 HD2 B:TYR98 4.8 27.5 1.0 H B:GLY94 4.8 27.1 1.0 N A:TYR64 4.9 19.0 1.0 CE2 B:TYR98 4.9 21.6 1.0 HA2 B:GLY94 4.9 29.6 1.0 CA A:TYR64 5.0 23.2 1.0 SG A:CYS88 5.0 20.7 1.0 O A:HOH769 5.0 27.7 1.0 HB2 B:SER92 5.0 27.5 1.0

Iron binding site 4 out of 32 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:27.7 occ:1.00 FE4 A:CLF501 0.0 27.7 1.0 S3A A:CLF501 2.2 17.7 1.0 S4A A:CLF501 2.3 16.9 1.0 S1 A:CLF501 2.4 21.6 1.0 SG A:CYS88 2.4 20.7 1.0 FE1 A:CLF501 2.6 26.8 1.0 FE2 A:CLF501 2.6 26.4 1.0 FE3 A:CLF501 2.7 31.9 1.0 FE5 A:CLF501 3.0 30.3 1.0 HB3 A:CYS88 3.1 29.1 1.0 CB A:CYS88 3.4 24.2 1.0 S2A A:CLF501 3.8 18.9 1.0 HB3 A:GLU153 3.8 24.0 1.0 H A:CYS154 3.9 30.1 1.0 HG2 A:GLU153 4.0 23.3 1.0 FE8 A:CLF501 4.0 33.0 1.0 HB2 A:CYS88 4.1 29.1 1.0 HA A:CYS88 4.3 29.9 1.0 S4B A:CLF501 4.3 20.0 1.0 HB3 A:TYR64 4.4 24.4 1.0 CA A:CYS88 4.4 24.9 1.0 HA A:GLU153 4.5 26.8 1.0 H A:CYS88 4.5 27.9 1.0 HE2 B:TYR98 4.6 25.9 1.0 CB A:GLU153 4.6 20.0 1.0 CG A:GLU153 4.6 19.4 1.0 HA3 A:GLY185 4.6 29.6 1.0 HD2 B:TYR98 4.7 27.5 1.0 HB2 A:CYS154 4.7 21.5 1.0 HD1 A:TYR64 4.7 23.2 1.0 CD1 A:TYR64 4.8 19.4 1.0 HB2 A:TYR64 4.8 24.4 1.0 SG B:CYS95 4.8 16.4 1.0 N A:CYS154 4.8 25.1 1.0 CG A:TYR64 4.8 22.6 1.0 SG A:CYS154 4.8 19.4 1.0 N A:CYS88 4.8 23.2 1.0 FE6 A:CLF501 4.9 30.4 1.0 SG A:CYS62 4.9 21.1 1.0 CB A:TYR64 4.9 20.3 1.0 S2B A:CLF501 4.9 17.6 1.0 CD A:GLU153 5.0 23.3 1.0

Iron binding site 5 out of 32 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:30.3 occ:1.00 FE5 A:CLF501 0.0 30.3 1.0 S2B A:CLF501 2.2 17.6 1.0 SG A:CYS88 2.3 20.7 1.0 S4B A:CLF501 2.3 20.0 1.0 H A:CYS88 2.6 27.9 1.0 S1 A:CLF501 2.7 21.6 1.0 FE8 A:CLF501 2.8 33.0 1.0 FE7 A:CLF501 2.8 31.5 1.0 FE4 A:CLF501 3.0 27.7 1.0 FE6 A:CLF501 3.0 30.4 1.0 N A:CYS88 3.1 23.2 1.0 HA3 A:GLY87 3.5 24.3 1.0 CB A:CYS88 3.5 24.2 1.0 HA A:CYS88 3.5 29.9 1.0 CA A:CYS88 3.6 24.9 1.0 FE1 A:CLF501 3.8 26.8 1.0 HB3 A:CYS88 3.9 29.1 1.0 C A:GLY87 3.9 22.4 1.0 S3A A:CLF501 3.9 17.7 1.0 CA A:GLY87 4.1 20.2 1.0 S3B A:CLF501 4.1 18.6 1.0 HB2 A:CYS88 4.2 29.1 1.0 H A:GLY87 4.3 18.7 1.0 HE2 A:TYR91 4.4 23.4 1.0 N A:GLY87 4.5 15.6 1.0 OE1 A:GLU153 4.6 20.7 1.0 HB2 A:PRO85 4.6 24.4 1.0 HD2 A:TYR91 4.7 24.1 1.0 HB3 A:GLU153 4.7 24.0 1.0 SG B:CYS95 4.8 16.4 1.0 FE2 A:CLF501 4.8 26.4 1.0 O A:GLY87 4.9 19.0 1.0 HD2 A:PRO85 4.9 23.5 1.0 HA2 A:GLY87 4.9 24.3 1.0 SG B:CYS153 4.9 19.3 1.0 SG B:CYS70 5.0 14.7 1.0 HD2 B:TYR98 5.0 27.5 1.0

Iron binding site 6 out of 32 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:30.4 occ:1.00 FE6 A:CLF501 0.0 30.4 1.0 S2B A:CLF501 2.3 17.6 1.0 S3B A:CLF501 2.3 18.6 1.0 SG B:CYS153 2.4 19.3 1.0 FE7 A:CLF501 2.7 31.5 1.0 FE8 A:CLF501 2.8 33.0 1.0 HB3 B:CYS153 2.9 19.9 1.0 S1 A:CLF501 3.0 21.6 1.0 FE5 A:CLF501 3.0 30.3 1.0 H B:CYS153 3.1 22.0 1.0 HB3 B:ALA188 3.1 26.7 1.0 CB B:CYS153 3.2 16.6 1.0 HG2 A:PRO85 3.3 25.3 1.0 HB2 B:ALA188 3.4 26.7 1.0 CB B:ALA188 3.5 22.3 1.0 HB1 B:ALA188 3.5 26.7 1.0 HB2 A:PRO85 3.7 24.4 1.0 N B:CYS153 3.8 18.3 1.0 HB2 B:CYS153 3.9 19.9 1.0 S4B A:CLF501 4.0 20.0 1.0 CA B:CYS153 4.2 16.1 1.0 CG A:PRO85 4.2 21.1 1.0 HD2 A:PRO85 4.3 23.5 1.0 CB A:PRO85 4.4 20.3 1.0 O B:HOH822 4.4 20.6 1.0 HB B:THR152 4.4 23.2 1.0 O B:HOH813 4.6 21.4 1.0 SG A:CYS88 4.7 20.7 1.0 HB2 A:CYS154 4.7 21.5 1.0 HD3 A:PRO155 4.7 23.4 1.0 HA B:CYS153 4.8 19.3 1.0 HB3 A:PRO85 4.8 24.4 1.0 CD A:PRO85 4.8 19.6 1.0 HA B:THR152 4.8 20.3 1.0 SG B:CYS95 4.9 16.4 1.0 HG3 A:PRO85 4.9 25.3 1.0 FE4 A:CLF501 4.9 27.7 1.0 HA3 A:GLY87 4.9 24.3 1.0 SG B:CYS70 4.9 14.7 1.0 H B:MET154 4.9 28.4 1.0 HB2 B:CYS70 5.0 20.5 1.0

Iron binding site 7 out of 32 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:31.5 occ:1.00 FE7 A:CLF501 0.0 31.5 1.0 S2B A:CLF501 2.2 17.6 1.0 S4B A:CLF501 2.3 20.0 1.0 S3B A:CLF501 2.4 18.6 1.0 SG B:CYS70 2.4 14.7 1.0 FE6 A:CLF501 2.7 30.4 1.0 FE8 A:CLF501 2.7 33.0 1.0 FE5 A:CLF501 2.8 30.3 1.0 HA3 A:GLY87 3.0 24.3 1.0 HB2 B:ALA188 3.4 26.7 1.0 HB1 B:ALA188 3.4 26.7 1.0 CB B:CYS70 3.5 17.1 1.0 HB3 B:CYS70 3.5 20.5 1.0 HB2 B:CYS70 3.5 20.5 1.0 HE2 A:TYR91 3.5 23.4 1.0 HZ B:PHE99 3.8 28.3 1.0 CB B:ALA188 3.8 22.3 1.0 HG2 B:PRO72 3.9 28.5 1.0 HE1 B:PHE99 3.9 22.0 1.0 CA A:GLY87 3.9 20.2 1.0 H A:GLY87 4.0 18.7 1.0 HB3 B:ALA188 4.1 26.7 1.0 HH A:TYR91 4.1 20.8 1.0 S1 A:CLF501 4.3 21.6 1.0 HD2 B:PRO72 4.3 27.0 1.0 H A:CYS88 4.3 27.9 1.0 HG3 B:PRO72 4.3 28.5 1.0 HB3 B:CYS95 4.4 26.2 1.0 HA2 A:GLY87 4.4 24.3 1.0 CE2 A:TYR91 4.4 19.5 1.0 CZ B:PHE99 4.5 23.6 1.0 N A:GLY87 4.5 15.6 1.0 CG B:PRO72 4.5 23.8 1.0 HB2 A:PRO85 4.5 24.4 1.0 CE1 B:PHE99 4.5 18.3 1.0 N A:CYS88 4.6 23.2 1.0 C A:GLY87 4.6 22.4 1.0 H B:CYS153 4.8 22.0 1.0 CD B:PRO72 4.9 22.5 1.0 CA B:CYS70 4.9 18.9 1.0 OH A:TYR91 4.9 17.3 1.0 SG B:CYS95 5.0 16.4 1.0 HB3 B:CYS153 5.0 19.9 1.0

Iron binding site 8 out of 32 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:33.0 occ:1.00 FE8 A:CLF501 0.0 33.0 1.0 S3B A:CLF501 2.3 18.6 1.0 S4B A:CLF501 2.3 20.0 1.0 SG B:CYS95 2.3 16.4 1.0 S1 A:CLF501 2.4 21.6 1.0 FE7 A:CLF501 2.7 31.5 1.0 FE5 A:CLF501 2.8 30.3 1.0 FE6 A:CLF501 2.8 30.4 1.0 HB3 B:CYS95 2.9 26.2 1.0 FE1 A:CLF501 2.9 26.8 1.0 CB B:CYS95 3.2 21.8 1.0 HB B:THR152 3.5 23.2 1.0 S2B A:CLF501 3.7 17.6 1.0 HA B:CYS95 3.8 27.2 1.0 HB2 B:CYS95 3.9 26.2 1.0 HZ B:PHE99 4.0 28.3 1.0 H B:CYS153 4.0 22.0 1.0 FE4 A:CLF501 4.0 27.7 1.0 CA B:CYS95 4.1 22.7 1.0 O B:HOH822 4.1 20.6 1.0 CB B:THR152 4.4 19.4 1.0 S3A A:CLF501 4.4 17.7 1.0 FE2 A:CLF501 4.4 26.4 1.0 SG B:CYS153 4.4 19.3 1.0 HG22 B:THR152 4.5 24.0 1.0 HA B:THR152 4.5 20.3 1.0 CZ B:PHE99 4.6 23.6 1.0 H B:CYS95 4.6 27.9 1.0 N B:CYS95 4.7 23.2 1.0 HG21 B:THR152 4.7 24.0 1.0 SG A:CYS88 4.8 20.7 1.0 CG2 B:THR152 4.8 20.0 1.0 N B:CYS153 4.8 18.3 1.0 HE1 B:PHE99 4.8 22.0 1.0 HE2 A:TYR91 4.9 23.4 1.0 SG B:CYS70 4.9 14.7 1.0 S2A A:CLF501 4.9 18.9 1.0 HG3 B:PRO72 5.0 28.5 1.0 HG2 B:PRO72 5.0 28.5 1.0

Iron binding site 9 out of 32 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe503 b:29.9 occ:1.00 FE1 A:ICS503 0.0 29.9 1.0 S2A A:ICS503 2.3 18.3 1.0 S4A A:ICS503 2.3 16.9 1.0 S1A A:ICS503 2.3 18.6 1.0 SG A:CYS275 2.3 23.2 1.0 FE4 A:ICS503 2.7 27.1 1.0 FE2 A:ICS503 2.7 27.9 1.0 FE3 A:ICS503 2.7 27.4 1.0 HB2 A:CYS275 3.1 28.4 1.0 CB A:CYS275 3.3 23.7 1.0 CX A:ICS503 3.5 7.2 1.0 HG A:SER278 3.5 26.7 1.0 HB3 A:SER278 3.5 28.9 1.0 HB3 A:LEU358 3.7 25.0 1.0 HB3 A:CYS275 3.7 28.4 1.0 HE2 A:TYR229 3.7 24.5 1.0 HB2 A:LEU358 3.7 25.0 1.0 HD22 A:LEU358 4.0 28.4 1.0 OG A:SER278 4.0 22.2 1.0 CB A:LEU358 4.2 20.9 1.0 CB A:SER278 4.3 24.1 1.0 H A:SER278 4.3 28.6 1.0 HB3 A:ARG277 4.4 34.1 1.0 HD23 A:LEU358 4.4 28.4 1.0 CE2 A:TYR229 4.5 20.4 1.0 CA A:CYS275 4.6 21.6 1.0 CD2 A:LEU358 4.6 23.6 1.0 HA A:CYS275 4.6 26.0 1.0 HD2 A:TYR229 4.7 24.7 1.0 H A:LEU358 4.8 30.0 1.0 HH A:TYR229 4.8 29.7 1.0 S2B A:ICS503 4.8 15.5 1.0 S3A A:ICS503 4.8 17.6 1.0 S5A A:ICS503 4.8 13.3 1.0 HB2 A:SER278 4.9 28.9 1.0 N A:SER278 4.9 23.8 1.0 N A:LEU358 5.0 25.0 1.0 H A:GLY357 5.0 23.9 1.0 FE6 A:ICS503 5.0 23.9 1.0 CD2 A:TYR229 5.0 20.6 1.0

Iron binding site 10 out of 32 in the Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii in the Dithionite Reduced State After Redox Cycling within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe503 b:27.9 occ:1.00 FE2 A:ICS503 0.0 27.9 1.0 CX A:ICS503 2.0 7.2 1.0 S2B A:ICS503 2.2 15.5 1.0 S2A A:ICS503 2.2 18.3 1.0 S1A A:ICS503 2.3 18.6 1.0 FE6 A:ICS503 2.6 23.9 1.0 FE4 A:ICS503 2.7 27.1 1.0 FE1 A:ICS503 2.7 29.9 1.0 FE3 A:ICS503 2.7 27.4 1.0 HZ A:PHE381 3.3 25.0 1.0 HE1 A:HIS195 3.7 30.1 1.0 FE5 A:ICS503 3.7 28.6 1.0 FE7 A:ICS503 3.7 25.0 1.0 HG11 A:VAL70 3.7 23.9 1.0 S4A A:ICS503 3.9 16.9 1.0 HE2 A:HIS195 3.9 29.4 1.0 HB3 A:SER278 4.1 28.9 1.0 HE1 A:PHE381 4.1 31.9 1.0 CE1 A:HIS195 4.1 25.1 1.0 CZ A:PHE381 4.2 20.8 1.0 S1B A:ICS503 4.2 12.8 1.0 S3B A:ICS503 4.2 12.6 1.0 HG13 A:VAL70 4.2 23.9 1.0 NE2 A:HIS195 4.2 24.5 1.0 HG21 A:VAL70 4.4 25.9 1.0 CG1 A:VAL70 4.4 19.9 1.0 S3A A:ICS503 4.5 17.6 1.0 S5A A:ICS503 4.5 13.3 1.0 H A:GLY357 4.5 23.9 1.0 HH11 A:ARG96 4.6 31.6 1.0 CE1 A:PHE381 4.6 26.6 1.0 HG22 A:VAL70 4.7 25.9 1.0 SG A:CYS275 4.7 23.2 1.0 HA3 A:GLY356 4.8 25.9 1.0 CB A:SER278 4.9 24.1 1.0 CG2 A:VAL70 5.0 21.6 1.0

H.L.Rutledge, J.Rittle, L.M.Williamson, W.A.Xu, D.M.Gagnon, F.A.Tezcan. Redox-Dependent Metastability of the Nitrogenase P-Cluster. J.Am.Chem.Soc. V. 141 10091 2019.
ISSN: ESSN 1520-5126
PubMed: 31146522
DOI: 10.1021/JACS.9B04555