Iron in PDB 5e44: Crystal Structure of Holo-Fnr of A. Fischeri

The structure of Crystal Structure of Holo-Fnr of A. Fischeri, PDB code: 5e44 was solved by A.Volbeda, J.C.Fontecilla-Camps, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.95 / 2.65
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	75.500, 75.500, 218.100, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 24.2

The binding sites of Iron atom in the Crystal Structure of Holo-Fnr of A. Fischeri (pdb code 5e44). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Holo-Fnr of A. Fischeri, PDB code: 5e44:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Holo-Fnr of A. Fischeri


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Holo-Fnr of A. Fischeri within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:0.2 occ:1.00 FE1 A:SF4301 0.0 0.2 1.0 S2 A:SF4301 2.3 0.1 1.0 S3 A:SF4301 2.3 0.1 1.0 S4 A:SF4301 2.3 0.7 1.0 SG A:CYS20 2.4 0.9 1.0 FE4 A:SF4301 2.7 0.4 1.0 FE3 A:SF4301 2.7 0.3 1.0 FE2 A:SF4301 2.8 0.0 1.0 CB A:CYS20 3.8 0.3 1.0 S1 A:SF4301 3.9 1.0 1.0 O A:CYS20 3.9 0.2 1.0 CA A:CYS20 4.4 0.2 1.0 CG A:PRO31 4.5 0.4 1.0 C A:CYS20 4.6 0.8 1.0 SG A:CYS122 4.7 0.2 1.0 SG A:CYS23 4.8 0.1 1.0 SG A:CYS29 4.8 0.5 1.0 CD A:PRO31 4.8 0.3 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Holo-Fnr of A. Fischeri


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Holo-Fnr of A. Fischeri within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:0.0 occ:1.00 FE2 A:SF4301 0.0 0.0 1.0 S4 A:SF4301 2.3 0.7 1.0 SG A:CYS23 2.3 0.1 1.0 S1 A:SF4301 2.3 1.0 1.0 S3 A:SF4301 2.3 0.1 1.0 FE3 A:SF4301 2.7 0.3 1.0 FE4 A:SF4301 2.7 0.4 1.0 FE1 A:SF4301 2.8 0.2 1.0 CB A:CYS23 3.2 0.4 1.0 S2 A:SF4301 3.9 0.1 1.0 CD A:ARG72 4.0 0.8 1.0 NE A:ARG72 4.4 0.1 1.0 O A:CYS20 4.5 0.2 1.0 CA A:CYS23 4.6 0.7 1.0 SG A:CYS20 4.6 0.9 1.0 CG1 A:ILE25 4.7 0.6 1.0 SG A:CYS29 4.7 0.5 1.0 O A:ASP22 4.9 0.1 1.0 SG A:CYS122 4.9 0.2 1.0 CD1 A:ILE25 5.0 0.6 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Holo-Fnr of A. Fischeri


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Holo-Fnr of A. Fischeri within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:0.3 occ:1.00 FE3 A:SF4301 0.0 0.3 1.0 S4 A:SF4301 2.3 0.7 1.0 S1 A:SF4301 2.3 1.0 1.0 S2 A:SF4301 2.3 0.1 1.0 SG A:CYS29 2.4 0.5 1.0 FE2 A:SF4301 2.7 0.0 1.0 FE1 A:SF4301 2.7 0.2 1.0 FE4 A:SF4301 2.8 0.4 1.0 CB A:CYS29 3.5 0.3 1.0 S3 A:SF4301 3.9 0.1 1.0 CB A:ALA70 4.1 93.0 1.0 CG2 A:ILE30 4.4 0.9 1.0 CD A:PRO31 4.5 0.3 1.0 SG A:CYS23 4.5 0.1 1.0 N A:ILE30 4.6 0.5 1.0 SG A:CYS122 4.8 0.2 1.0 CA A:CYS29 4.9 0.5 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Holo-Fnr of A. Fischeri


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Holo-Fnr of A. Fischeri within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:0.4 occ:1.00 FE4 A:SF4301 0.0 0.4 1.0 S3 A:SF4301 2.3 0.1 1.0 S2 A:SF4301 2.3 0.1 1.0 S1 A:SF4301 2.3 1.0 1.0 SG A:CYS122 2.3 0.2 1.0 FE1 A:SF4301 2.7 0.2 1.0 FE2 A:SF4301 2.7 0.0 1.0 FE3 A:SF4301 2.8 0.3 1.0 CB A:CYS122 3.3 0.1 1.0 S4 A:SF4301 3.9 0.7 1.0 CD A:ARG72 4.0 0.8 1.0 SG A:CYS20 4.5 0.9 1.0 CB A:ARG72 4.6 0.2 1.0 CB A:ALA70 4.7 93.0 1.0 CA A:CYS122 4.7 0.8 1.0 NE A:ARG72 4.8 0.1 1.0 CG A:ARG72 4.9 0.8 1.0 SG A:CYS23 4.9 0.1 1.0 CA A:ARG72 4.9 0.0 1.0 CB A:GLU47 4.9 0.4 1.0 SG A:CYS29 5.0 0.5 1.0 N A:CYS122 5.0 0.3 1.0

A.Volbeda, C.Darnault, O.Renoux, Y.Nicolet, J.C.Fontecilla-Camps. The Crystal Structure of the Global Anaerobic Transcriptional Regulator Fnr Explains Its Extremely Fine-Tuned Monomer-Dimer Equilibrium. Sci Adv V. 1 01086 2015.
ISSN: ESSN 2375-2548
PubMed: 26665177
DOI: 10.1126/SCIADV.1501086