Molybdenum 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
Iron	(Fe)	30 atoms

The binding sites of Molybdenum 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 Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation, PDB code: 8e3u:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Nickel-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 Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo603 b:29.7 occ:1.00 MO1 A:ICS603 0.0 29.7 1.0 S4B A:ICS603 2.2 33.9 1.0 ND1 A:HIS442 2.4 22.7 1.0 O7 A:HCA602 2.4 48.4 1.0 S3B A:ICS603 2.4 28.5 1.0 S1B A:ICS603 2.4 31.0 1.0 O6 A:HCA602 2.6 28.2 1.0 FE7 A:ICS603 2.7 24.3 1.0 FE6 A:ICS603 2.7 33.5 1.0 FE5 A:ICS603 2.8 34.9 1.0 HB3 A:HIS442 3.1 34.6 1.0 CE1 A:HIS442 3.2 33.9 1.0 C7 A:HCA602 3.2 36.7 1.0 C3 A:HCA602 3.3 41.1 1.0 HE1 A:HIS442 3.3 40.7 1.0 H52 A:HCA602 3.3 41.1 1.0 CG A:HIS442 3.4 31.8 1.0 CX A:ICS603 3.7 26.3 1.0 CB A:HIS442 3.8 28.8 1.0 H22 A:HCA602 4.0 56.1 1.0 C2 A:HCA602 4.2 46.8 1.0 C5 A:HCA602 4.2 34.3 1.0 O A:HOH861 4.3 28.7 1.0 C4 A:HCA602 4.3 46.0 1.0 O5 A:HCA602 4.4 32.0 1.0 NE2 A:HIS442 4.4 33.8 1.0 HA A:HIS442 4.4 31.8 1.0 HD2 A:ARG96 4.4 44.0 1.0 HB2 A:HIS442 4.5 34.6 1.0 CD2 A:HIS442 4.5 30.0 1.0 O2 A:HCA602 4.5 34.5 1.0 H41 A:HCA602 4.7 55.2 1.0 H51 A:HCA602 4.7 41.1 1.0 CA A:HIS442 4.7 26.5 1.0 HG22 A:ILE355 4.7 43.1 1.0 S2B A:ICS603 4.8 31.6 1.0 HH11 A:ARG96 4.8 39.5 1.0 C1 A:HCA602 4.9 48.1 1.0 S5A A:ICS603 4.9 24.8 1.0

Molybdenum binding site 2 out of 2 in the Nickel-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 Nickel-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo603 b:34.0 occ:1.00 MO1 C:ICS603 0.0 34.0 1.0 S4B C:ICS603 2.2 41.4 1.0 S3B C:ICS603 2.4 41.4 1.0 O7 C:HCA602 2.4 53.3 1.0 S1B C:ICS603 2.4 36.0 1.0 ND1 C:HIS442 2.4 41.5 1.0 O5 C:HCA602 2.6 26.8 1.0 FE6 C:ICS603 2.7 31.2 1.0 FE7 C:ICS603 2.7 31.3 1.0 FE5 C:ICS603 2.8 28.4 1.0 HB3 C:HIS442 3.0 37.6 1.0 H52 C:HCA602 3.2 41.9 1.0 C7 C:HCA602 3.2 39.0 1.0 C3 C:HCA602 3.3 50.4 1.0 CE1 C:HIS442 3.4 37.9 1.0 CG C:HIS442 3.4 34.3 1.0 HE1 C:HIS442 3.5 45.5 1.0 CX C:ICS603 3.6 40.5 1.0 CB C:HIS442 3.7 31.4 1.0 C5 C:HCA602 4.0 34.9 1.0 O C:HOH860 4.3 25.9 1.0 C4 C:HCA602 4.3 48.5 1.0 H51 C:HCA602 4.3 41.9 1.0 O6 C:HCA602 4.3 38.0 1.0 HB2 C:HIS442 4.3 37.6 1.0 H22 C:HCA602 4.3 67.0 1.0 C2 C:HCA602 4.4 55.8 1.0 HD2 C:ARG96 4.4 50.0 1.0 HA C:HIS442 4.4 34.2 1.0 NE2 C:HIS442 4.5 30.4 1.0 O1 C:HCA602 4.6 60.1 1.0 CD2 C:HIS442 4.6 22.9 1.0 H41 C:HCA602 4.7 58.2 1.0 HH11 C:ARG96 4.7 50.4 1.0 CA C:HIS442 4.7 28.5 1.0 HG22 C:ILE355 4.7 41.2 1.0 S2B C:ICS603 4.8 30.8 1.0 C1 C:HCA602 4.9 54.8 1.0 S5A C:ICS603 4.9 31.7 1.0 HD3 C:ARG96 5.0 50.0 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