Iron in PDB 5x5p: Human Serum Transferrin Bound to Ruthenium Nta

The structure of Human Serum Transferrin Bound to Ruthenium Nta, PDB code: 5x5p was solved by H.Sun, M.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.26 / 2.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	136.748, 158.395, 106.610, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 21.9

The structure of Human Serum Transferrin Bound to Ruthenium Nta also contains other interesting chemical elements:

Ruthenium	(Ru)	4 atoms
Sodium	(Na)	1 atom

The binding sites of Iron atom in the Human Serum Transferrin Bound to Ruthenium Nta (pdb code 5x5p). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Human Serum Transferrin Bound to Ruthenium Nta, PDB code: 5x5p:

Iron binding site 1 out of 1 in the Human Serum Transferrin Bound to Ruthenium Nta


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Serum Transferrin Bound to Ruthenium Nta within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe702 b:50.0 occ:1.00 O9 A:MLI701 1.9 49.9 1.0 O7 A:MLI701 2.0 49.0 1.0 OH A:TYR517 2.0 60.8 1.0 OD2 A:ASP392 2.2 57.4 1.0 OH A:TYR426 2.3 62.1 1.0 NE2 A:HIS585 2.4 58.3 1.0 C3 A:MLI701 3.0 44.6 1.0 C2 A:MLI701 3.0 39.6 1.0 CE1 A:HIS585 3.1 49.1 1.0 CZ A:TYR517 3.2 41.3 1.0 CG A:ASP392 3.2 42.1 1.0 CZ A:TYR426 3.4 63.8 1.0 CD2 A:HIS585 3.4 67.1 1.0 C1 A:MLI701 3.5 37.4 1.0 CB A:ASP392 3.7 43.3 1.0 CE1 A:TYR517 4.0 38.3 1.0 O8 A:MLI701 4.0 48.6 1.0 CE2 A:TYR517 4.0 36.9 1.0 O6 A:MLI701 4.1 41.7 1.0 CE2 A:TYR426 4.2 59.4 1.0 CE1 A:TYR426 4.2 61.0 1.0 OD1 A:ASP392 4.2 46.0 1.0 ND1 A:HIS585 4.3 58.9 1.0 CB A:THR457 4.3 59.4 1.0 CG A:HIS585 4.4 59.4 1.0 CA A:ASP392 4.4 46.9 1.0 OG1 A:THR457 4.5 60.4 1.0 N A:ALA458 4.6 44.7 1.0 N A:THR457 4.7 46.5 1.0 O A:HOH807 4.7 44.3 1.0 N A:GLY393 4.9 47.6 1.0

H.Sun, M.Wang, Q.Hao. The Additional Metal-Binding Site on Human Serum Transferrin Surface To Be Published.