Iron in PDB 5jac: Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A

All present enzymatic activity of Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A:
1.16.3.1;

The structure of Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A, PDB code: 5jac was solved by C.Pozzi, F.Di Pisa, S.Mangani, C.Bernacchioni, P.Turano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.63 / 1.18
Space group	F 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	184.372, 184.372, 184.372, 90.00, 90.00, 90.00
R / Rfree (%)	12.1 / 13.4

The structure of Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A also contains other interesting chemical elements:

Magnesium	(Mg)	9 atoms
Chlorine	(Cl)	14 atoms

The binding sites of Iron atom in the Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A (pdb code 5jac). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A, PDB code: 5jac:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:10.6 occ:0.60 O A:HOH312 2.0 16.4 0.6 OE1 A:GLU23 2.0 12.1 1.0 OE1 A:GLU58 2.0 16.6 1.0 O A:HOH310 2.2 14.5 1.0 ND1 A:HIS61 2.2 13.3 0.9 CD A:GLU23 2.9 10.9 1.0 CD A:GLU58 3.0 14.3 1.0 CE1 A:HIS61 3.1 14.2 0.9 O A:HOH461 3.1 17.9 0.5 OE2 A:GLU23 3.2 13.5 1.0 CG A:HIS61 3.3 12.2 0.9 OE2 A:GLU58 3.5 19.9 1.0 FE A:FE2202 3.5 12.7 0.5 CB A:HIS61 3.7 10.2 1.0 OE1 A:GLN137 4.1 11.9 0.4 CG1 A:VAL106 4.1 12.7 1.0 OE1 A:GLN137 4.1 15.5 0.5 NE2 A:HIS61 4.2 15.2 0.9 O A:HOH452 4.3 17.0 1.0 CG A:GLU23 4.3 10.2 1.0 CG A:GLU58 4.3 12.8 1.0 CD2 A:HIS61 4.4 13.3 0.9 CA A:GLU58 4.4 10.1 1.0 CB A:GLU58 4.6 10.8 1.0 O A:HOH470 4.7 25.7 0.5 O A:HOH306 4.7 22.1 0.6 CB A:GLU23 4.7 9.0 1.0 CD A:GLN137 4.8 13.0 0.4 NE2 A:GLN137 4.8 16.1 0.5 CD A:GLN137 4.9 13.4 0.5 O A:HOH342 4.9 20.1 0.5

Iron binding site 2 out of 3 in the Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:12.7 occ:0.50 OE2 A:GLU58 1.8 19.9 1.0 O A:HOH312 1.9 16.4 0.6 O A:HOH470 2.0 25.7 0.5 OE2 A:GLU103 2.3 18.4 0.9 OE1 A:GLU103 2.3 16.7 0.9 O A:HOH461 2.4 17.9 0.5 CD A:GLU103 2.6 13.5 0.9 CD A:GLU58 2.9 14.3 1.0 OE1 A:GLU58 3.2 16.6 1.0 O A:HOH342 3.3 20.1 0.5 FE A:FE2201 3.5 10.6 0.6 OE1 A:GLN137 3.6 11.9 0.4 NE2 A:GLN137 3.9 16.1 0.5 O A:HOH306 4.0 22.1 0.6 CG A:GLU58 4.1 12.8 1.0 CG A:GLU103 4.1 11.5 1.0 NE2 A:GLN137 4.2 15.1 0.4 OE1 A:GLN137 4.3 15.5 0.5 CD A:GLN137 4.3 13.0 0.4 CE1 A:HIS61 4.3 14.2 0.9 CE2 A:TYR30 4.4 12.4 0.8 CE2 A:TYR30 4.5 11.6 0.2 CD A:GLN137 4.5 13.4 0.5 ND1 A:HIS61 4.6 13.3 0.9 O A:HOH310 4.6 14.5 1.0 OH A:TYR30 4.7 15.9 0.8 O A:HOH575 4.7 27.0 0.6 OH A:TYR30 4.8 13.4 0.2 ND1 A:HIS54 4.8 20.6 0.4 CB A:GLU103 5.0 9.7 1.0

Iron binding site 3 out of 3 in the Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Sixty Minutes Iron Loaded Rana Catesbeiana H' Ferritin Variant E57A/E136A/D140A within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe203 b:10.3 occ:0.15 CL A:CL205 2.2 15.3 0.2 NE2 A:HIS169 2.3 13.2 0.8 CE1 A:HIS169 3.1 12.2 0.8 CD2 A:HIS169 3.5 14.1 0.8 O A:HOH579 3.7 28.4 0.2 ND1 A:HIS169 4.3 11.9 0.8 CG A:HIS169 4.5 11.7 0.8

C.Bernacchioni, C.Pozzi, F.Di Pisa, S.Mangani, P.Turano. Ferroxidase Activity in Eukaryotic Ferritin Is Controlled By Accessory-Iron-Binding Sites in the Catalytic Cavity. Chemistry V. 22 16213 2016.
ISSN: ISSN 0947-6539
PubMed: 27650996
DOI: 10.1002/CHEM.201602842