Iron in PDB 6op4: Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii

All present enzymatic activity of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii:
1.18.6.1;

The structure of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii, PDB code: 6op4 was solved by R.J.Arias, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.41 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	76.981, 129.326, 106.755, 90.00, 108.84, 90.00
R / Rfree (%)	17.6 / 22.3

The structure of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Magnesium	(Mg)	2 atoms
Calcium	(Ca)	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 Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii (pdb code 6op4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 30 binding sites of Iron where determined in the Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii, PDB code: 6op4:
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 Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:21.4 occ:1.00 FE1 A:ICS502 0.0 21.4 1.0 SG A:CYS275 2.2 21.7 1.0 S2A A:ICS502 2.3 20.6 1.0 S4A A:ICS502 2.3 21.1 1.0 S1A A:ICS502 2.3 21.6 1.0 FE3 A:ICS502 2.7 20.6 1.0 FE2 A:ICS502 2.7 20.7 1.0 FE4 A:ICS502 2.7 19.9 1.0 CB A:CYS275 3.2 20.7 1.0 CX A:ICS502 3.4 19.5 1.0 OG A:SER278 4.1 21.3 1.0 CB A:LEU358 4.1 24.2 1.0 CB A:SER278 4.3 20.9 1.0 CE2 A:TYR229 4.4 22.2 1.0 CA A:CYS275 4.4 22.3 1.0 CD2 A:LEU358 4.7 22.9 1.0 S5A A:ICS502 4.8 18.7 1.0 CD2 A:TYR229 4.8 22.6 1.0 S3A A:ICS502 4.9 17.1 1.0 S2B A:ICS502 4.9 17.9 1.0 N A:SER278 4.9 21.8 1.0 FE7 A:ICS502 5.0 20.0 1.0 FE6 A:ICS502 5.0 19.5 1.0 CG A:LEU358 5.0 23.4 1.0

Iron binding site 2 out of 30 in the Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:20.7 occ:1.00 FE2 A:ICS502 0.0 20.7 1.0 CX A:ICS502 2.0 19.5 1.0 S2A A:ICS502 2.3 20.6 1.0 S1A A:ICS502 2.3 21.6 1.0 S2B A:ICS502 2.3 17.9 1.0 FE6 A:ICS502 2.6 19.5 1.0 FE4 A:ICS502 2.6 19.9 1.0 FE1 A:ICS502 2.7 21.4 1.0 FE3 A:ICS502 2.7 20.6 1.0 FE5 A:ICS502 3.7 20.8 1.0 FE7 A:ICS502 3.7 20.0 1.0 S4A A:ICS502 3.9 21.1 1.0 CZ A:PHE381 4.0 17.0 1.0 NE2 A:HIS195 4.1 25.7 1.0 S3B A:ICS502 4.2 20.5 1.0 S1B A:ICS502 4.2 20.0 1.0 CE1 A:HIS195 4.2 27.6 1.0 CG1 A:VAL70 4.3 23.0 1.0 S3A A:ICS502 4.5 17.1 1.0 CE1 A:PHE381 4.5 16.9 1.0 S5A A:ICS502 4.5 18.7 1.0 SG A:CYS275 4.5 21.7 1.0 CG2 A:VAL70 5.0 22.2 1.0 N A:GLY357 5.0 18.9 1.0

Iron binding site 3 out of 30 in the Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:20.6 occ:1.00 FE3 A:ICS502 0.0 20.6 1.0 CX A:ICS502 2.0 19.5 1.0 S5A A:ICS502 2.2 18.7 1.0 S4A A:ICS502 2.3 21.1 1.0 S2A A:ICS502 2.3 20.6 1.0 FE7 A:ICS502 2.6 20.0 1.0 FE1 A:ICS502 2.7 21.4 1.0 FE4 A:ICS502 2.7 19.9 1.0 FE2 A:ICS502 2.7 20.7 1.0 FE6 A:ICS502 3.7 19.5 1.0 FE5 A:ICS502 3.7 20.8 1.0 S1A A:ICS502 3.9 21.6 1.0 NH2 A:ARG96 3.9 21.3 1.0 CD2 A:TYR229 4.1 22.6 1.0 O A:HOH755 4.1 23.3 1.0 S3B A:ICS502 4.2 20.5 1.0 S4B A:ICS502 4.2 20.4 1.0 CE2 A:TYR229 4.4 22.2 1.0 S2B A:ICS502 4.5 17.9 1.0 S3A A:ICS502 4.5 17.1 1.0 SG A:CYS275 4.7 21.7 1.0 CG A:TYR229 5.0 22.4 1.0

Iron binding site 4 out of 30 in the Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:19.9 occ:1.00 FE4 A:ICS502 0.0 19.9 1.0 CX A:ICS502 2.0 19.5 1.0 S3A A:ICS502 2.3 17.1 1.0 S1A A:ICS502 2.3 21.6 1.0 S4A A:ICS502 2.3 21.1 1.0 FE5 A:ICS502 2.6 20.8 1.0 FE2 A:ICS502 2.6 20.7 1.0 FE3 A:ICS502 2.7 20.6 1.0 FE1 A:ICS502 2.7 21.4 1.0 FE7 A:ICS502 3.7 20.0 1.0 FE6 A:ICS502 3.7 19.5 1.0 S2A A:ICS502 3.8 20.6 1.0 CB A:LEU358 4.0 24.2 1.0 N A:LEU358 4.0 23.1 1.0 N A:GLY357 4.0 18.9 1.0 S4B A:ICS502 4.2 20.4 1.0 S1B A:ICS502 4.3 20.0 1.0 S5A A:ICS502 4.5 18.7 1.0 SG A:CYS275 4.6 21.7 1.0 S2B A:ICS502 4.6 17.9 1.0 CA A:LEU358 4.6 23.0 1.0 CA A:GLY357 4.6 21.5 1.0 C A:GLY357 4.6 23.5 1.0 N A:ARG359 4.6 24.1 1.0 CG A:ARG359 4.7 23.3 1.0 CD A:ARG359 4.8 21.8 1.0 CA A:GLY356 4.9 18.9 1.0 C A:GLY356 5.0 19.0 1.0 CZ A:PHE381 5.0 17.0 1.0 NE A:ARG359 5.0 23.2 1.0

Iron binding site 5 out of 30 in the Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:20.8 occ:1.00 FE5 A:ICS502 0.0 20.8 1.0 CX A:ICS502 2.0 19.5 1.0 S4B A:ICS502 2.2 20.4 1.0 S1B A:ICS502 2.2 20.0 1.0 S3A A:ICS502 2.3 17.1 1.0 FE4 A:ICS502 2.6 19.9 1.0 FE6 A:ICS502 2.6 19.5 1.0 FE7 A:ICS502 2.6 20.0 1.0 MO1 A:ICS502 2.7 19.9 1.0 FE2 A:ICS502 3.7 20.7 1.0 ND1 A:HIS442 3.7 17.9 1.0 FE3 A:ICS502 3.7 20.6 1.0 S3B A:ICS502 3.8 20.5 1.0 CE1 A:HIS442 4.1 19.5 1.0 N A:GLY356 4.1 18.4 1.0 CA A:GLY356 4.2 18.9 1.0 CG2 A:ILE355 4.2 19.0 1.0 S1A A:ICS502 4.3 21.6 1.0 S4A A:ICS502 4.4 21.1 1.0 S5A A:ICS502 4.5 18.7 1.0 S2B A:ICS502 4.5 17.9 1.0 O7 A:HCA501 4.6 21.8 1.0 CD A:ARG359 4.7 21.8 1.0 CG A:HIS442 4.7 17.9 1.0 O6 A:HCA501 4.7 21.5 1.0 N A:GLY357 4.7 18.9 1.0 CZ A:PHE381 5.0 17.0 1.0

Iron binding site 6 out of 30 in the Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:19.5 occ:1.00 FE6 A:ICS502 0.0 19.5 1.0 CX A:ICS502 2.0 19.5 1.0 S2B A:ICS502 2.2 17.9 1.0 S3B A:ICS502 2.2 20.5 1.0 S1B A:ICS502 2.2 20.0 1.0 FE2 A:ICS502 2.6 20.7 1.0 FE7 A:ICS502 2.6 20.0 1.0 FE5 A:ICS502 2.6 20.8 1.0 MO1 A:ICS502 2.7 19.9 1.0 FE3 A:ICS502 3.7 20.6 1.0 FE4 A:ICS502 3.7 19.9 1.0 S4B A:ICS502 3.8 20.4 1.0 O7 A:HCA501 3.9 21.8 1.0 CZ A:PHE381 4.1 17.0 1.0 S2A A:ICS502 4.2 20.6 1.0 S1A A:ICS502 4.3 21.6 1.0 CG2 A:VAL70 4.3 22.2 1.0 O2 A:HCA501 4.4 26.5 1.0 S5A A:ICS502 4.4 18.7 1.0 O6 A:HCA501 4.5 21.5 1.0 CE2 A:PHE381 4.5 17.3 1.0 S3A A:ICS502 4.5 17.1 1.0 ND1 A:HIS442 4.7 17.9 1.0 C3 A:HCA501 4.8 24.4 1.0 C2 A:HCA501 4.9 26.0 1.0 C7 A:HCA501 5.0 23.1 1.0 FE1 A:ICS502 5.0 21.4 1.0 CG1 A:VAL70 5.0 23.0 1.0 C1 A:HCA501 5.0 26.4 1.0

Iron binding site 7 out of 30 in the Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:20.0 occ:1.00 FE7 A:ICS502 0.0 20.0 1.0 CX A:ICS502 2.0 19.5 1.0 S5A A:ICS502 2.2 18.7 1.0 S3B A:ICS502 2.2 20.5 1.0 S4B A:ICS502 2.2 20.4 1.0 FE3 A:ICS502 2.6 20.6 1.0 FE6 A:ICS502 2.6 19.5 1.0 FE5 A:ICS502 2.6 20.8 1.0 MO1 A:ICS502 2.7 19.9 1.0 O A:HOH684 3.6 24.2 1.0 FE2 A:ICS502 3.7 20.7 1.0 FE4 A:ICS502 3.7 19.9 1.0 O6 A:HCA501 3.8 21.5 1.0 S1B A:ICS502 3.8 20.0 1.0 NE A:ARG96 4.0 20.5 1.0 NH2 A:ARG96 4.1 21.3 1.0 S2A A:ICS502 4.3 20.6 1.0 S4A A:ICS502 4.3 21.1 1.0 S2B A:ICS502 4.5 17.9 1.0 S3A A:ICS502 4.5 17.1 1.0 CZ A:ARG96 4.6 19.2 1.0 ND1 A:HIS442 4.6 17.9 1.0 C7 A:HCA501 4.7 23.1 1.0 O7 A:HCA501 4.7 21.8 1.0 CZ A:ARG359 4.8 25.9 1.0 NH1 A:ARG359 4.9 23.8 1.0 CD A:ARG96 4.9 20.7 1.0 FE1 A:ICS502 5.0 21.4 1.0 NH2 A:ARG359 5.0 24.6 1.0

Iron binding site 8 out of 30 in the Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe505 b:22.3 occ:1.00 FE1 A:CLF505 0.0 22.3 1.0 S2A A:CLF505 1.5 32.2 1.0 S3A A:CLF505 1.9 20.6 1.0 SG A:CYS154 2.4 21.4 1.0 S1 A:CLF505 2.4 21.9 1.0 FE4 A:CLF505 2.5 19.6 1.0 FE2 A:CLF505 2.5 20.0 1.0 FE3 A:CLF505 2.9 18.9 1.0 CB A:CYS154 3.4 20.9 1.0 S4A A:CLF505 3.5 21.7 1.0 N A:CYS154 3.7 19.8 1.0 O B:HOH838 3.8 20.8 1.0 CA A:GLY185 4.0 26.0 1.0 CA A:CYS154 4.0 22.6 1.0 N A:GLY185 4.1 23.5 1.0 SG B:CYS95 4.2 21.8 1.0 FE8 A:CLF505 4.4 19.4 1.0 FE5 A:CLF505 4.4 20.7 1.0 SG A:CYS88 4.5 22.3 1.0 CB B:SER92 4.7 26.0 1.0 FE6 A:CLF505 4.7 24.2 1.0 OG B:SER92 4.8 30.5 1.0 C A:GLY185 4.8 25.9 1.0 C A:GLU153 4.8 20.8 1.0 SG B:CYS153 4.9 20.5 1.0 SG A:CYS62 4.9 20.4 1.0

Iron binding site 9 out of 30 in the Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe505 b:20.0 occ:1.00 FE2 A:CLF505 0.0 20.0 1.0 S2A A:CLF505 2.0 32.2 1.0 S4A A:CLF505 2.1 21.7 1.0 SG B:CYS95 2.4 21.8 1.0 FE4 A:CLF505 2.4 19.6 1.0 S1 A:CLF505 2.4 21.9 1.0 FE1 A:CLF505 2.5 22.3 1.0 FE3 A:CLF505 2.7 18.9 1.0 FE8 A:CLF505 2.9 19.4 1.0 N B:CYS95 3.3 22.4 1.0 S3A A:CLF505 3.4 20.6 1.0 CA B:CYS95 3.6 22.9 1.0 CB B:CYS95 3.6 21.1 1.0 FE5 A:CLF505 3.7 20.7 1.0 S4B A:CLF505 3.9 19.6 1.0 C B:GLY94 3.9 23.2 1.0 CA B:GLY94 4.4 22.1 1.0 SG A:CYS88 4.4 22.3 1.0 O B:HOH838 4.4 20.8 1.0 SG A:CYS154 4.5 21.4 1.0 FE6 A:CLF505 4.5 24.2 1.0 CB B:SER92 4.6 26.0 1.0 O B:GLY94 4.6 23.6 1.0 SG A:CYS62 4.7 20.4 1.0 N B:GLY94 4.9 21.2 1.0 O B:SER92 5.0 24.1 1.0

Iron binding site 10 out of 30 in the Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Selenium-Incorporated, Carbon Monoxide-Inhibited, Reactivated Femo- Cofactor of Nitrogenase From Azotobacter Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe505 b:18.9 occ:1.00 FE3 A:CLF505 0.0 18.9 1.0 S4A A:CLF505 2.0 21.7 1.0 S3A A:CLF505 2.2 20.6 1.0 S2A A:CLF505 2.2 32.2 1.0 SG A:CYS62 2.3 20.4 1.0 FE4 A:CLF505 2.6 19.6 1.0 FE2 A:CLF505 2.7 20.0 1.0 FE1 A:CLF505 2.9 22.3 1.0 CB A:CYS62 3.2 22.0 1.0 CA A:GLY185 4.0 26.0 1.0 CB A:TYR64 4.1 18.9 1.0 CA B:GLY94 4.1 22.1 1.0 S1 A:CLF505 4.3 21.9 1.0 C B:GLY94 4.3 23.2 1.0 N B:CYS95 4.5 22.4 1.0 CD1 A:TYR64 4.6 19.4 1.0 N A:GLY185 4.6 23.5 1.0 O B:HOH845 4.6 24.7 1.0 CA A:CYS62 4.6 22.3 1.0 CG A:TYR64 4.7 20.3 1.0 SG A:CYS154 4.8 21.4 1.0 SG A:CYS88 4.9 22.3 1.0 O A:HOH700 4.9 21.2 1.0 CE2 B:TYR98 4.9 20.6 1.0 O B:GLY94 4.9 23.6 1.0 N A:TYR64 4.9 19.7 1.0 SG B:CYS95 4.9 21.8 1.0 N B:GLY94 5.0 21.2 1.0

J.T.Henthorn, R.J.Arias, S.Koroidov, T.Kroll, D.Sokaras, U.Bergmann, D.C.Rees, S.Debeer. Localized Electronic Structure of Nitrogenase Femoco Revealed By Selenium K-Edge High Resolution X-Ray Absorption Spectroscopy. J.Am.Chem.Soc. V. 141 13676 2019.
ISSN: ESSN 1520-5126
PubMed: 31356071
DOI: 10.1021/JACS.9B06988