Molybdenum in PDB 8e3t: Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation

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

The structure of Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation, PDB code: 8e3t 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)	54.13 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	76.607, 127.968, 107.269, 90, 108.85, 90
R / Rfree (%)	22.3 / 24.3

The structure of Gallium-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 Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation (pdb code 8e3t). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Gallium-Reconstituted Nitrogenase Mofep Mutant S188A From Azotobacter Vinelandii After Ids Oxidation, PDB code: 8e3t:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Gallium-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 Gallium-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:25.1 occ:1.00 MO1 A:ICS502 0.0 25.1 1.0 S1B A:ICS502 2.3 29.0 1.0 S4B A:ICS502 2.4 29.0 1.0 S3B A:ICS502 2.4 30.3 1.0 O7 A:HCA501 2.4 29.9 1.0 ND1 A:HIS442 2.6 27.7 1.0 O6 A:HCA501 2.6 26.8 1.0 FE6 A:ICS502 2.7 25.2 1.0 FE7 A:ICS502 2.7 31.0 1.0 FE5 A:ICS502 2.7 22.9 1.0 C7 A:HCA501 3.2 28.3 1.0 HE1 A:HIS442 3.3 34.2 1.0 CE1 A:HIS442 3.3 28.5 1.0 C3 A:HCA501 3.3 28.9 1.0 CX A:ICS502 3.5 25.2 1.0 H52 A:HCA501 3.5 33.6 1.0 HB3 A:HIS442 3.6 31.5 1.0 CG A:HIS442 3.7 26.6 1.0 O A:HOH675 3.9 25.3 1.0 H22 A:HCA501 4.0 36.4 1.0 CB A:HIS442 4.1 26.2 1.0 HA A:HIS442 4.1 29.4 1.0 HE A:ARG96 4.2 33.3 1.0 C2 A:HCA501 4.3 30.3 1.0 O5 A:HCA501 4.3 30.2 1.0 C4 A:HCA501 4.4 29.7 1.0 C5 A:HCA501 4.4 28.0 1.0 NE2 A:HIS442 4.5 28.3 1.0 H41 A:HCA501 4.6 35.7 1.0 HG22 A:ILE355 4.6 35.7 1.0 CA A:HIS442 4.7 24.4 1.0 HA3 A:GLY356 4.7 34.5 1.0 CD2 A:HIS442 4.7 27.4 1.0 O A:HOH743 4.7 34.9 1.0 S2B A:ICS502 4.8 29.2 1.0 O2 A:HCA501 4.8 32.8 1.0 S5A A:ICS502 4.8 25.5 1.0 S3A A:ICS502 4.9 27.2 1.0 HB2 A:HIS442 5.0 31.5 1.0 H A:GLY356 5.0 35.0 1.0

Molybdenum binding site 2 out of 2 in the Gallium-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 Gallium-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:52.5 occ:1.00 MO1 C:ICS502 0.0 52.5 1.0 S1B C:ICS502 2.3 30.9 1.0 S4B C:ICS502 2.3 31.5 1.0 S3B C:ICS502 2.4 36.5 1.0 O7 C:HCA501 2.4 32.2 1.0 O5 C:HCA501 2.5 28.4 1.0 ND1 C:HIS442 2.6 29.1 1.0 FE7 C:ICS502 2.7 32.3 1.0 FE6 C:ICS502 2.7 27.6 1.0 FE5 C:ICS502 2.7 26.7 1.0 C7 C:HCA501 3.3 29.7 1.0 HB3 C:HIS442 3.3 32.3 1.0 C3 C:HCA501 3.4 32.0 1.0 CE1 C:HIS442 3.4 29.8 1.0 HE1 C:HIS442 3.5 35.7 1.0 CX C:ICS502 3.5 26.3 1.0 H52 C:HCA501 3.6 34.7 1.0 CG C:HIS442 3.6 27.8 1.0 O C:HOH687 3.9 27.2 1.0 CB C:HIS442 3.9 26.9 1.0 HA C:HIS442 4.0 31.5 1.0 H22 C:HCA501 4.3 38.6 1.0 O1 C:HCA501 4.3 33.7 1.0 C2 C:HCA501 4.4 32.1 1.0 C4 C:HCA501 4.4 30.5 1.0 O6 C:HCA501 4.4 30.9 1.0 C5 C:HCA501 4.5 28.9 1.0 HG22 C:ILE355 4.5 34.5 1.0 HD2 C:ARG96 4.5 35.5 1.0 CA C:HIS442 4.6 26.2 1.0 NE2 C:HIS442 4.6 29.4 1.0 H41 C:HCA501 4.7 36.6 1.0 CD2 C:HIS442 4.7 28.2 1.0 HB2 C:HIS442 4.8 32.3 1.0 S2B C:ICS502 4.8 27.8 1.0 S5A C:ICS502 4.8 24.4 1.0 C1 C:HCA501 4.8 33.7 1.0 HH11 C:ARG96 4.8 34.6 1.0 HA3 C:GLY356 4.9 36.2 1.0 S3A C:ICS502 4.9 28.7 1.0 HD3 C:ARG96 4.9 35.5 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