Iron in PDB 29ki: Spinach Ferredoxin I, Reduced, -400 Mv

The structure of Spinach Ferredoxin I, Reduced, -400 Mv, PDB code: 29ki was solved by S.Laxmi, S.B.Carr, K.A.Vincent, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.55 / 1.11
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	30.02, 51.55, 61.09, 90, 90, 90
R / Rfree (%)	16.6 / 19.4

The binding sites of Iron atom in the Spinach Ferredoxin I, Reduced, -400 Mv (pdb code 29ki). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Spinach Ferredoxin I, Reduced, -400 Mv, PDB code: 29ki:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Spinach Ferredoxin I, Reduced, -400 Mv


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Spinach Ferredoxin I, Reduced, -400 Mv within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe101 b:14.8 occ:1.00 FE1 A:FES101 0.0 14.8 1.0 S2 A:FES101 2.2 14.6 1.0 S1 A:FES101 2.3 15.2 1.0 SG A:CYS44 2.3 16.0 1.0 SG A:CYS39 2.3 15.5 1.0 FE2 A:FES101 2.7 13.9 1.0 H A:CYS39 2.9 19.6 1.0 H A:ARG40 3.1 19.0 1.0 H A:CYS44 3.2 17.5 1.0 CB A:CYS44 3.3 15.6 1.0 HB3 A:CYS44 3.4 18.7 1.0 CB A:CYS39 3.5 16.4 1.0 HB3 A:CYS39 3.5 19.7 1.0 N A:CYS39 3.6 16.3 1.0 N A:CYS44 3.6 14.6 1.0 H A:ALA41 3.6 17.7 1.0 H A:SER43 3.7 17.2 1.0 N A:ARG40 3.7 15.8 1.0 HB2 A:SER46 3.7 18.1 0.6 CA A:CYS44 3.8 14.9 1.0 H A:GLY42 3.8 17.8 1.0 HB3 A:SER46 3.9 20.6 0.4 H A:SER38 3.9 19.9 0.4 H A:SER46 3.9 18.0 0.4 H A:SER46 3.9 18.0 0.6 H A:SER38 3.9 19.9 0.6 CA A:CYS39 3.9 16.8 1.0 C A:CYS44 4.0 15.1 1.0 O A:CYS44 4.0 15.5 1.0 HB3 A:SER38 4.2 23.4 0.6 HB2 A:CYS44 4.2 18.7 1.0 HG A:SER38 4.2 19.2 0.4 C A:CYS39 4.2 16.6 1.0 H A:CYS47 4.2 17.5 1.0 HB2 A:CYS39 4.3 19.7 1.0 N A:SER43 4.3 14.3 1.0 SG A:CYS77 4.4 13.8 1.0 HA A:ARG40 4.4 19.2 1.0 OG A:SER38 4.4 16.0 0.4 N A:ALA41 4.4 14.7 1.0 C A:SER43 4.5 14.9 1.0 N A:GLY42 4.5 14.8 1.0 SG A:CYS47 4.6 13.2 1.0 N A:SER46 4.6 15.0 1.0 CA A:ARG40 4.6 16.0 1.0 C A:SER38 4.7 17.6 1.0 N A:SER38 4.7 16.6 1.0 CB A:SER46 4.7 15.1 0.6 N A:SER45 4.7 14.9 1.0 HA A:CYS44 4.7 17.9 1.0 CB A:SER46 4.7 17.1 0.4 HB3 A:CYS47 4.8 17.5 1.0 HD13 A:LEU75 4.8 17.4 1.0 HA A:CYS39 4.8 20.2 1.0 HA2 A:GLY42 4.8 16.4 1.0 HB2 A:SER46 4.9 20.6 0.4 C A:GLY42 5.0 14.0 1.0 N A:CYS47 5.0 14.6 1.0 H A:SER45 5.0 17.9 1.0 CB A:SER38 5.0 19.5 0.6

Iron binding site 2 out of 2 in the Spinach Ferredoxin I, Reduced, -400 Mv


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Spinach Ferredoxin I, Reduced, -400 Mv within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe101 b:13.9 occ:1.00 FE2 A:FES101 0.0 13.9 1.0 S2 A:FES101 2.2 14.6 1.0 S1 A:FES101 2.2 15.2 1.0 SG A:CYS47 2.3 13.2 1.0 SG A:CYS77 2.3 13.8 1.0 FE1 A:FES101 2.7 14.8 1.0 HB3 A:CYS77 2.9 17.4 1.0 HB3 A:CYS47 3.1 17.5 1.0 CB A:CYS77 3.2 14.5 1.0 CB A:CYS47 3.3 14.6 1.0 H A:CYS77 3.4 15.8 1.0 HB3 A:LEU75 3.5 14.7 1.0 H A:GLY42 3.5 17.8 1.0 H A:CYS47 3.6 17.5 1.0 HA A:ARG40 3.7 19.2 1.0 H A:ARG40 3.8 19.0 1.0 HB2 A:CYS77 3.8 17.4 1.0 HB2 A:CYS47 3.9 17.5 1.0 HA2 A:GLY42 4.1 16.4 1.0 N A:CYS77 4.1 13.2 1.0 H A:ALA41 4.2 17.7 1.0 CA A:CYS77 4.3 14.0 1.0 N A:CYS47 4.3 14.6 1.0 N A:GLY42 4.3 14.8 1.0 HD13 A:LEU75 4.3 17.4 1.0 N A:ARG40 4.4 15.8 1.0 HD22 A:LEU75 4.4 19.2 1.0 SG A:CYS39 4.4 15.5 1.0 CA A:CYS47 4.4 14.1 1.0 CA A:ARG40 4.4 16.0 1.0 CB A:LEU75 4.5 12.2 1.0 H A:CYS44 4.6 17.5 1.0 HB2 A:SER46 4.6 18.1 0.6 SG A:CYS44 4.6 16.0 1.0 H A:SER38 4.6 19.9 0.6 H A:SER38 4.6 19.9 0.4 N A:ALA41 4.7 14.7 1.0 HB3 A:SER46 4.7 20.6 0.4 CA A:GLY42 4.7 13.6 1.0 HA A:TYR37 4.7 19.9 1.0 HB2 A:TYR37 4.8 22.1 1.0 O A:CYS44 4.8 15.5 1.0 HA A:LEU75 4.8 14.4 1.0 C A:ARG40 4.8 16.2 1.0 H A:SER43 4.9 17.2 1.0 H A:CYS39 4.9 19.6 1.0 HD22 A:LEU25 5.0 20.5 1.0 C A:CYS77 5.0 13.3 1.0 HB2 A:LEU75 5.0 14.7 1.0 HA A:CYS77 5.0 16.8 1.0

S.Laxmi, S.Jaho, W.K.Myers, K.A.Vincent, S.B.Carr. Crystallise, Poise, Capture: A Multimodal Platform For Correlated Structural and Spectroscopic Characterisation of Redox Enzymes. J.Biol.Inorg.Chem. 2026.
ISSN: ESSN 1432-1327
PubMed: 42082801
DOI: 10.1007/S00775-026-02148-X