Iron in PDB 6n4l: Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii

All present enzymatic activity of Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii:
1.18.6.1;

The structure of Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii, PDB code: 6n4l was solved by B.B.Wenke, T.Spatzal, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.04 / 1.13
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.587, 74.630, 75.398, 90.00, 90.00, 90.00
R / Rfree (%)	14.6 / 15.7

The structure of Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Iron atom in the Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii (pdb code 6n4l). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii, PDB code: 6n4l:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe303 b:12.2 occ:1.00 FE1 A:SF4303 0.0 12.2 1.0 S3 A:SF4303 2.2 12.5 1.0 SG A:CYS97 2.3 16.0 1.0 S4 A:SF4303 2.3 13.0 1.0 FE2 A:SF4303 2.7 12.2 1.0 CB A:CYS97 3.3 16.6 1.0 CA A:CYS97 3.8 15.9 1.0 N A:ALA98 4.2 12.3 1.0 C A:CYS97 4.3 13.4 1.0 CA A:GLY133 4.5 13.8 1.0 N A:GLY99 4.7 10.4 1.0 N A:GLY133 4.8 13.4 1.0 SG A:CYS132 4.8 14.0 1.0

Iron binding site 2 out of 2 in the Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Dithionite-Reduced Adp-Bound Form of the Nitrogenase Fe-Protein From A. Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe303 b:12.2 occ:1.00 FE2 A:SF4303 0.0 12.2 1.0 S4 A:SF4303 2.3 13.0 1.0 S3 A:SF4303 2.3 12.5 1.0 SG A:CYS132 2.3 14.0 1.0 FE1 A:SF4303 2.7 12.2 1.0 CB A:CYS132 3.4 13.4 1.0 C A:CYS132 4.1 12.3 1.0 CG2 A:VAL130 4.2 13.0 1.0 O A:CYS132 4.3 12.5 1.0 CA A:CYS132 4.3 12.5 1.0 N A:GLY133 4.4 13.4 1.0 SG A:CYS97 4.8 16.0 1.0 CB A:VAL130 4.8 12.5 1.0 N A:CYS132 4.9 11.7 1.0 CA A:GLY133 5.0 13.8 1.0

B.B.Wenke, T.Spatzal, D.C.Rees. Site-Specific Oxidation State Assignments of the Iron Atoms in the [4FE:4S]2+/1+/0STATES of the Nitrogenase Fe-Protein. Angew. Chem. Int. Ed. Engl. V. 58 3894 2019.
ISSN: ESSN 1521-3773
PubMed: 30698901
DOI: 10.1002/ANIE.201813966