Molybdenum in PDB 8e3v: Cobalt-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation

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

The structure of Cobalt-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation, PDB code: 8e3v 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)	80.17 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	77.127, 130.039, 107.76, 90, 109.12, 90
R / Rfree (%)	18.2 / 20.8

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

Iron

(Fe)

32 atoms

The binding sites of Molybdenum atom in the Cobalt-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation (pdb code 8e3v). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Cobalt-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation, PDB code: 8e3v:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Cobalt-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Cobalt-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo502 b:17.9 occ:1.00 MO1 A:ICS502 0.0 17.9 1.0 S4B A:ICS502 2.3 18.6 1.0 S1B A:ICS502 2.3 15.8 1.0 S3B A:ICS502 2.3 17.2 1.0 O7 A:HCA501 2.4 18.1 1.0 O6 A:HCA501 2.4 20.5 1.0 ND1 A:HIS442 2.4 18.3 1.0 FE6 A:ICS502 2.7 21.4 1.0 FE7 A:ICS502 2.7 20.7 1.0 FE5 A:ICS502 2.7 21.4 1.0 C7 A:HCA501 3.1 20.0 1.0 CE1 A:HIS442 3.2 21.3 1.0 C3 A:HCA501 3.2 19.9 1.0 HE1 A:HIS442 3.3 25.6 1.0 HB3 A:HIS442 3.3 22.8 1.0 H52 A:HCA501 3.5 25.6 1.0 CG A:HIS442 3.5 18.0 1.0 CX A:ICS502 3.5 16.1 1.0 CB A:HIS442 3.8 19.0 1.0 O A:HOH737 4.0 22.1 1.0 H22 A:HCA501 4.1 28.1 1.0 HA A:HIS442 4.2 23.2 1.0 C2 A:HCA501 4.2 23.4 1.0 O2 A:HCA501 4.2 22.7 1.0 O5 A:HCA501 4.2 20.0 1.0 C5 A:HCA501 4.3 21.3 1.0 C4 A:HCA501 4.3 21.6 1.0 NE2 A:HIS442 4.4 19.4 1.0 HE A:ARG96 4.5 27.8 1.0 H41 A:HCA501 4.5 25.9 1.0 HG22 A:ILE355 4.5 27.0 1.0 CD2 A:HIS442 4.5 21.1 1.0 CA A:HIS442 4.6 19.3 1.0 HB2 A:HIS442 4.6 22.8 1.0 H51 A:HCA501 4.7 25.6 1.0 C1 A:HCA501 4.7 28.5 1.0 S2B A:ICS502 4.7 16.1 1.0 S5A A:ICS502 4.8 17.3 1.0 HG3 A:ARG96 4.8 30.3 1.0 HA3 A:GLY356 4.8 26.2 1.0 S3A A:ICS502 4.9 19.9 1.0 HG23 A:ILE355 5.0 27.0 1.0

Molybdenum binding site 2 out of 2 in the Cobalt-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Cobalt-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo502 b:19.4 occ:1.00 MO1 C:ICS502 0.0 19.4 1.0 S4B C:ICS502 2.3 19.5 1.0 S3B C:ICS502 2.3 18.3 1.0 S1B C:ICS502 2.3 17.4 1.0 O7 C:HCA501 2.4 17.2 1.0 ND1 C:HIS442 2.4 18.0 1.0 O5 C:HCA501 2.4 20.5 1.0 FE6 C:ICS502 2.7 22.1 1.0 FE7 C:ICS502 2.7 21.2 1.0 FE5 C:ICS502 2.7 21.6 1.0 C7 C:HCA501 3.0 19.6 1.0 CE1 C:HIS442 3.2 18.2 1.0 C3 C:HCA501 3.2 21.1 1.0 HE1 C:HIS442 3.2 21.8 1.0 HB3 C:HIS442 3.4 25.4 1.0 CG C:HIS442 3.5 17.9 1.0 CX C:ICS502 3.5 16.6 1.0 H22 C:HCA501 3.8 22.8 1.0 H52 C:HCA501 3.8 24.8 1.0 CB C:HIS442 3.9 21.2 1.0 O C:HOH745 3.9 29.0 1.0 C2 C:HCA501 4.1 19.0 1.0 HE C:ARG96 4.1 35.3 1.0 HA C:HIS442 4.1 24.5 1.0 O6 C:HCA501 4.2 27.0 1.0 C4 C:HCA501 4.3 19.9 1.0 O1 C:HCA501 4.3 27.6 1.0 NE2 C:HIS442 4.4 22.8 1.0 HG22 C:ILE355 4.4 31.9 1.0 H41 C:HCA501 4.5 23.9 1.0 HD2 C:ARG96 4.5 30.9 1.0 CD2 C:HIS442 4.5 17.8 1.0 C5 C:HCA501 4.6 20.7 1.0 CA C:HIS442 4.6 20.4 1.0 HB2 C:HIS442 4.7 25.4 1.0 C1 C:HCA501 4.7 23.8 1.0 S2B C:ICS502 4.8 18.9 1.0 S5A C:ICS502 4.8 20.5 1.0 H21 C:HCA501 4.9 22.8 1.0 HA3 C:GLY356 4.9 26.4 1.0 S3A C:ICS502 4.9 18.5 1.0 NE C:ARG96 5.0 29.4 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