Iron in PDB 5lg8: Human L-Type Ferritin Iron Loaded For 60 Minutes

The structure of Human L-Type Ferritin Iron Loaded For 60 Minutes, PDB code: 5lg8 was solved by C.Pozzi, F.Di Pisa, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.70 / 1.98
Space group	I 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	151.420, 151.420, 151.420, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 17.7

The structure of Human L-Type Ferritin Iron Loaded For 60 Minutes also contains other interesting chemical elements:

Cadmium

(Cd)

8 atoms

The binding sites of Iron atom in the Human L-Type Ferritin Iron Loaded For 60 Minutes (pdb code 5lg8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Human L-Type Ferritin Iron Loaded For 60 Minutes, PDB code: 5lg8:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Human L-Type Ferritin Iron Loaded For 60 Minutes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human L-Type Ferritin Iron Loaded For 60 Minutes within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe209 b:38.8 occ:1.00 O1 A:OXY213 1.8 28.7 1.0 OE2 A:GLU61 2.0 47.9 1.0 OE2 A:GLU64 2.1 31.0 1.0 O1 A:PER214 2.3 43.0 1.0 O A:HOH383 2.3 43.0 1.0 O2 A:PER216 2.3 41.7 1.0 CD A:GLU61 2.9 33.6 1.0 CD A:GLU64 3.1 31.3 1.0 O1 A:PER216 3.1 36.9 1.0 OE1 A:GLU61 3.2 35.3 1.0 O2 A:PER214 3.3 41.5 1.0 FE A:FE210 3.3 42.7 1.0 O A:HOH305 3.4 50.0 1.0 OE1 A:GLU64 3.4 33.8 1.0 FE A:FE211 3.5 39.6 1.0 O A:HOH322 4.0 54.6 1.0 CG A:GLU61 4.3 32.7 1.0 CG A:GLU64 4.5 27.4 1.0 OE1 A:GLU60 4.5 40.7 1.0 CB A:GLU64 4.9 20.5 1.0 O2 A:PER215 4.9 39.2 1.0 OE2 A:GLU60 5.0 37.0 1.0

Iron binding site 2 out of 4 in the Human L-Type Ferritin Iron Loaded For 60 Minutes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human L-Type Ferritin Iron Loaded For 60 Minutes within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe210 b:42.7 occ:1.00 O1 A:OXY213 2.0 28.7 1.0 OE2 A:GLU57 2.1 29.4 0.7 OE1 A:GLU60 2.3 40.7 1.0 OE1 A:GLU61 2.4 35.3 1.0 O1 A:PER216 2.4 36.9 1.0 O1 A:PER215 2.6 51.5 1.0 CD A:GLU57 3.1 29.4 0.7 O2 A:PER215 3.2 39.2 1.0 FE A:FE211 3.2 39.6 1.0 CD A:GLU60 3.2 39.3 1.0 O2 A:PER216 3.3 41.7 1.0 FE A:FE209 3.3 38.8 1.0 CD A:GLU61 3.4 33.6 1.0 OE1 A:GLU57 3.5 31.5 0.7 OE2 A:GLU60 3.5 37.0 1.0 O A:HOH388 3.6 51.2 1.0 OE2 A:GLU61 3.7 47.9 1.0 O A:HOH335 3.9 53.9 1.0 FE A:FE212 4.4 57.0 0.5 OE2 A:GLU64 4.4 31.0 1.0 CG A:GLU57 4.4 25.5 0.7 OE1 A:GLU64 4.4 33.8 1.0 CG A:GLU60 4.6 28.4 1.0 O1 A:PER214 4.6 43.0 1.0 CD A:GLU64 4.7 31.3 1.0 O A:GLU57 4.7 23.1 1.0 CG A:GLU61 4.7 32.7 1.0 O2 A:PER214 4.7 41.5 1.0 N A:GLU61 4.8 18.9 1.0 CB A:GLU60 4.9 19.5 1.0 CA A:GLU61 4.9 21.4 1.0 CB A:GLU61 4.9 22.2 1.0

Iron binding site 3 out of 4 in the Human L-Type Ferritin Iron Loaded For 60 Minutes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Human L-Type Ferritin Iron Loaded For 60 Minutes within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe211 b:39.6 occ:1.00 O1 A:OXY213 2.0 28.7 1.0 OE1 A:GLU64 2.1 33.8 1.0 O A:HOH382 2.2 40.4 1.0 OE2 A:GLU60 2.2 37.0 1.0 O2 A:PER215 2.4 39.2 1.0 O2 A:PER214 2.4 41.5 1.0 CD A:GLU64 3.1 31.3 1.0 CD A:GLU60 3.1 39.3 1.0 O1 A:PER214 3.2 43.0 1.0 FE A:FE210 3.2 42.7 1.0 OE1 A:GLU60 3.4 40.7 1.0 O1 A:PER215 3.4 51.5 1.0 FE A:FE209 3.5 38.8 1.0 OE2 A:GLU64 3.5 31.0 1.0 CG A:GLU64 4.3 27.4 1.0 O1 A:PER216 4.5 36.9 1.0 O A:HOH438 4.5 52.6 1.0 CG A:GLU60 4.5 28.4 1.0 O2 A:PER216 4.7 41.7 1.0 O A:HOH457 4.7 30.3 0.5 OE1 A:GLU61 4.8 35.3 1.0 OE2 A:GLU61 4.9 47.9 1.0

Iron binding site 4 out of 4 in the Human L-Type Ferritin Iron Loaded For 60 Minutes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Human L-Type Ferritin Iron Loaded For 60 Minutes within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe212 b:57.0 occ:0.50 OE1 A:GLU57 2.5 31.5 0.7 O A:HOH457 2.7 30.3 0.5 O A:HOH496 2.7 26.4 0.5 O1 A:PER215 2.9 51.5 1.0 CD A:GLU57 3.7 29.4 0.7 O2 A:PER215 3.7 39.2 1.0 CD A:GLU60 3.9 39.3 1.0 OE1 A:GLU60 3.9 40.7 1.0 OE2 A:GLU60 4.2 37.0 1.0 OE2 A:GLU57 4.2 29.4 0.7 CG A:GLU60 4.4 28.4 1.0 FE A:FE210 4.4 42.7 1.0 O A:HOH388 4.4 51.2 1.0 CB A:GLU60 4.6 19.5 1.0 CG A:GLU57 4.9 25.5 0.7 CA A:GLU57 5.0 20.2 1.0

C.Pozzi, S.Ciambellotti, C.Bernacchioni, F.Di Pisa, S.Mangani, P.Turano. Chemistry at the Protein-Mineral Interface in L-Ferritin Assists the Assembly of A Functional ( Mu (3)-Oxo)Tris[( Mu (2)-Peroxo)] Triiron(III) Cluster. Proc. Natl. Acad. Sci. V. 114 2580 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28202724
DOI: 10.1073/PNAS.1614302114